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Structures of membrane protein

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https://www.readbyqxmd.com/read/28231452/proteome-scale-identification-classification-and-structural-analysis-of-iron-binding-proteins-in-bread-wheat
#1
Shailender Kumar Verma, Ankita Sharma, Padmani Sandhu, Neha Choudhary, Shailaja Sharma, Vishal Acharya, Yusuf Akhter
Bread wheat is one of the major staple foods of worldwide population and iron plays a significant role in growth and development of the plant. In this report, we are presenting the genome wide identification of iron-binding proteins in bread wheat. The wheat genome derived putative proteome was screened for identification of iron-binding sequence motifs. Out of 602 putative iron-binding proteins, 130 were able to produce reliable structural models by homology techniques and further analyzed for the presence of iron-binding structural motifs...
February 14, 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28230992/novel-design-of-heptad-amphiphiles-to-enhance-cell-selectivity-salt-resistance-anti-biofilm-properties-and-their-membrane-disruptive-mechanism
#2
Xiujing Dou, Xin Zhu, Jiajun Wang, Na Dong, Anshan Shan
Coiled-coil, a basic folding pattern of native proteins, was previously demonstrated to be associated with the specific spatial recognition, association, and dissociation of proteins and can be used to perfect engineering peptide model. Thus, in this study, a series of amphiphiles composed of heptads repeats with coiled-coil structures was constructed, and the designed peptides exhibited a broad spectrum of antimicrobial activities. Circular dichroism and biological assays showed that the heptad repeats and length of the linker between the heptads largely influenced the amphiphile's helical propensity and cell selectivity...
February 23, 2017: Journal of Medicinal Chemistry
https://www.readbyqxmd.com/read/28230156/drebrin-mediated-microtubule-actomyosin-coupling-steers-cerebellar-granule-neuron-nucleokinesis-and-migration-pathway-selection
#3
Niraj Trivedi, Daniel R Stabley, Blake Cain, Danielle Howell, Christophe Laumonnerie, Joseph S Ramahi, Jamshid Temirov, Ryan A Kerekes, Phillip R Gordon-Weeks, David J Solecki
Neuronal migration from a germinal zone to a final laminar position is essential for the morphogenesis of neuronal circuits. While it is hypothesized that microtubule-actomyosin crosstalk is required for a neuron's 'two-stroke' nucleokinesis cycle, the molecular mechanisms controlling such crosstalk are not defined. By using the drebrin microtubule-actin crosslinking protein as an entry point into the cerebellar granule neuron system in combination with super-resolution microscopy, we investigate how these cytoskeletal systems interface during migration...
February 23, 2017: Nature Communications
https://www.readbyqxmd.com/read/28230084/highly-potent-antimicrobial-peptides-from-n-terminal-membrane-binding-region-of-e-coli-mreb
#4
Karabi Saikia, Yalavarthi Durga Sravani, Vibin Ramakrishnan, Nitin Chaudhary
Microbial pathogenesis is a serious health concern. The threat escalates as the existing conventional antimicrobials are losing their efficacy against the evolving pathogens. Peptides hold promise to be developed into next-generation antibiotics. Antimicrobial peptides adopt amphipathic structures that could selectively bind to and disrupt the microbial membranes. Interaction of proteins with membranes is central to all living systems and we reasoned that the membrane-binding domains in microbial proteins could be developed into efficient antimicrobials...
February 23, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28229180/erratum-to-high-resolution-structure-of-a-membrane-protein-transferred-from-amphipol-to-a-lipidic-mesophase
#5
V Polovinkin, I Gushchin, M Sintsov, E Round, T Balandin, P Chervakov, V Shevchenko, P Utrobin, A Popov, V Borshchevskiy, A Mishin, A Kuklin, D Willbold, V Chupin, J-L Popot, V Gordeliy
No abstract text is available yet for this article.
February 22, 2017: Journal of Membrane Biology
https://www.readbyqxmd.com/read/28228927/computational-approaches-for-revealing-the-structure-of-membrane-transporters-case-study-on-bilitranslocase
#6
REVIEW
Katja Venko, A Roy Choudhury, Marjana Novič
The structural and functional details of transmembrane proteins are vastly underexplored, mostly due to experimental difficulties regarding their solubility and stability. Currently, the majority of transmembrane protein structures are still unknown and this present a huge experimental and computational challenge. Nowadays, thanks to X-ray crystallography or NMR spectroscopy over 3000 structures of membrane proteins have been solved, among them only a few hundred unique ones. Due to the vast biological and pharmaceutical interest in the elucidation of the structure and the functional mechanisms of transmembrane proteins, several computational methods have been developed to overcome the experimental gap...
2017: Computational and Structural Biotechnology Journal
https://www.readbyqxmd.com/read/28228551/cysteine-residues-in-a-yeast-viral-a-b-toxin-crucially-control-host-cell-killing-via-ph-triggered-disulfide-rearrangements
#7
Yutaka Suzuki, Sara L Schwartz, Nina C Mueller, Manfred J Schmitt
K28 is a viral A/B protein toxin that intoxicates yeast and fungal cells by endocytosis and retrograde transport to the endoplasmic reticulum (ER). While toxin translocation into the cytosol occurs on the oxidized α/β heterodimer, the precise mechanism of how the toxin crosses the ER membrane is unknown. Here we identified pH-triggered toxin-intrinsic thiol rearrangements that crucially control toxin conformation and host cell killing. In the natural habitat and low pH environment of toxin-secreting killer yeasts, K28 is structurally stable and biologically active as disulfide-bonded heterodimer while it forms inactive disulfide-bonded oligomers at neutral pH that are caused by activation and thiol deprotonation of β-subunit cysteines...
February 22, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28228524/structural-insights-into-the-activation-mechanism-of-dynamin-like-ehd-atpases
#8
Arthur Alves Melo, Balachandra G Hegde, Claudio Shah, Elin Larsson, J Mario Isas, Séverine Kunz, Richard Lundmark, Ralf Langen, Oliver Daumke
Eps15 (epidermal growth factor receptor pathway substrate 15)-homology domain containing proteins (EHDs) comprise a family of dynamin-related mechano-chemical ATPases involved in cellular membrane trafficking. Previous studies have revealed the structure of the EHD2 dimer, but the molecular mechanisms of membrane recruitment and assembly have remained obscure. Here, we determined the crystal structure of an amino-terminally truncated EHD4 dimer. Compared with the EHD2 structure, the helical domains are 50° rotated relative to the GTPase domain...
February 22, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28228010/selective-fusion-of-heterogeneous-classifiers-for-predicting-substrates-of-membrane-transporters
#9
Naeem Shaikh, Mahesh Sharma, Prabha Garg
Membrane transporters play a crucial role in determining fate of administered drugs in a biological system. Early identification of plausible transporters for a drug molecule can provide insights into its therapeutic, pharmacokinetic and toxicological profile. In the present study, predictive models for classifying small molecules into substrates and non-substrates of various pharmaceutically important membrane transporters are developed using QSAR and proteochemometric (PCM) approaches. For this purpose, 4575 substrate interactions for these transporters were collected from Metabolism and Transport Database (Metrabase) and literature...
February 23, 2017: Journal of Chemical Information and Modeling
https://www.readbyqxmd.com/read/28226239/structural-basis-for-the-hijacking-of-endosomal-sorting-nexin-proteins-by-chlamydia-trachomatis
#10
Blessy Paul, Hyun Sung Kim, Markus C Kerr, Wilhelmina M Huston, Rohan D Teasdale, Brett M Collins
During infection chlamydial pathogens form an intracellular membrane-bound replicative niche termed the inclusion, which is enriched with bacterial transmembrane proteins called Incs. Incs bind and manipulate host cell proteins to promote inclusion expansion and provide camouflage against innate immune responses. Sorting nexin (SNX) proteins that normally function in endosomal membrane trafficking are a major class of inclusion-associated host proteins, and are recruited by IncE/CT116. Crystal structures of the SNX5 phox-homology (PX) domain in complex with IncE define the precise molecular basis for these interactions...
February 22, 2017: ELife
https://www.readbyqxmd.com/read/28225803/bacterial-expression-correct-membrane-targeting-and-functional-folding-of-the-hiv-1-membrane-protein-vpu-using-a-periplasmic-signal-peptide
#11
Arpan Deb, William A Johnson, Alexander P Kline, Boston J Scott, Lydia R Meador, Dustin Srinivas, Jose M Martin-Garcia, Katerina Dörner, Chad R Borges, Rajeev Misra, Brenda G Hogue, Petra Fromme, Tsafrir S Mor
Viral protein U (Vpu) is a type-III integral membrane protein encoded by Human Immunodeficiency Virus-1 (HIV- 1). It is expressed in infected host cells and plays several roles in viral progeny escape from infected cells, including down-regulation of CD4 receptors. But key structure/function questions remain regarding the mechanisms by which the Vpu protein contributes to HIV-1 pathogenesis. Here we describe expression of Vpu in bacteria, its purification and characterization. We report the successful expression of PelB-Vpu in Escherichia coli using the leader peptide pectate lyase B (PelB) from Erwinia carotovora...
2017: PloS One
https://www.readbyqxmd.com/read/28225760/reconstitution-of-the-tubular-endoplasmic-reticulum-network-with-purified-components
#12
Robert E Powers, Songyu Wang, Tina Y Liu, Tom A Rapoport
Organelles display characteristic morphologies that are intimately tied to their cellular function, but how organelles are shaped is poorly understood. The endoplasmic reticulum is particularly intriguing, as it comprises morphologically distinct domains, including a dynamic network of interconnected membrane tubules. Several membrane proteins have been implicated in network formation, but how exactly they mediate network formation and whether they are all required are unclear. Here we reconstitute a dynamic tubular membrane network with purified endoplasmic reticulum proteins...
February 22, 2017: Nature
https://www.readbyqxmd.com/read/28225603/reversible-lifting-of-surface-supported-lipid-bilayers-with-a-membrane-spanning-non-ionic-triblock-copolymer
#13
Steven C Hayden, Ann Junghans, Jaroslaw Majewski, Millicent Anne Firestone
Neutron reflectometry was used to monitor structural variations in surface supported DMPC bilayers induced by the addition of Triton X-100, a surfactant commonly used to aid solubilization of membrane proteins, and the co-addition of a membrane spanning non-ionic amphiphilic triblock copolymer, (PEO117-PPO47-PEO117, Pluronic F98). Surfactant addition causes slight compression of the bilayer thickness and the creation of a distinct EO layer that increases the hydrophilic layer proximal to the supporting substrate (i...
February 22, 2017: Biomacromolecules
https://www.readbyqxmd.com/read/28225081/biomolecular-condensates-organizers-of-cellular-biochemistry
#14
REVIEW
Salman F Banani, Hyun O Lee, Anthony A Hyman, Michael K Rosen
Biomolecular condensates are micron-scale compartments in eukaryotic cells that lack surrounding membranes but function to concentrate proteins and nucleic acids. These condensates are involved in diverse processes, including RNA metabolism, ribosome biogenesis, the DNA damage response and signal transduction. Recent studies have shown that liquid-liquid phase separation driven by multivalent macromolecular interactions is an important organizing principle for biomolecular condensates. With this physical framework, it is now possible to explain how the assembly, composition, physical properties and biochemical and cellular functions of these important structures are regulated...
February 22, 2017: Nature Reviews. Molecular Cell Biology
https://www.readbyqxmd.com/read/28225045/membrane-targeting-of-tirap-is-negatively-regulated-by-phosphorylation-in-its-phosphoinositide-binding-motif
#15
Xiaolin Zhao, Wen Xiong, Shuyan Xiao, Tuo-Xian Tang, Jeffrey F Ellena, Geoffrey S Armstrong, Carla V Finkielstein, Daniel G S Capelluto
Pathogen-activated Toll-like receptors (TLRs), such as TLR2 and TLR4, dimerize and move laterally across the plasma membrane to phosphatidylinositol (4,5)-bisphosphate-enriched domains. At these sites, TLRs interact with the TIR domain-containing adaptor protein (TIRAP), triggering a signaling cascade that leads to innate immune responses. Membrane recruitment of TIRAP is mediated by its phosphoinositide (PI)-binding motif (PBM). We show that TIRAP PBM transitions from a disordered to a helical conformation in the presence of either zwitterionic micelles or monodispersed PIs...
February 22, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28224491/predicting-alpha-helical-transmembrane-proteins-using-hmms
#16
Georgios N Tsaousis, Margarita C Theodoropoulou, Stavros J Hamodrakas, Pantelis G Bagos
Alpha helical transmembrane (TM) proteins constitute an important structural class of membrane proteins involved in a wide variety of cellular functions. The prediction of their transmembrane topology, as well as their discrimination in newly sequenced genomes, is of great importance for the elucidation of their structure and function. Several methods have been applied for the prediction of the transmembrane segments and the topology of alpha helical transmembrane proteins utilizing different algorithmic techniques...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28224490/predicting-beta-barrel-transmembrane-proteins-using-hmms
#17
Georgios N Tsaousis, Stavros J Hamodrakas, Pantelis G Bagos
Transmembrane beta-barrels (TMBBs) constitute an important structural class of membrane proteins located in the outer membrane of gram-negative bacteria, and in the outer membrane of chloroplasts and mitochondria. They are involved in a wide variety of cellular functions and the prediction of their transmembrane topology, as well as their discrimination in newly sequenced genomes is of great importance as they are promising targets for antimicrobial drugs and vaccines. Several methods have been applied for the prediction of the transmembrane segments and the topology of beta barrel transmembrane proteins utilizing different algorithmic techniques...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28224124/the-mammalian-septin-interactome
#18
REVIEW
Katharina Neubauer, Barbara Zieger
Septins are GTP-binding and membrane-interacting proteins with a highly conserved domain structure involved in various cellular processes, including cytoskeleton organization, cytokinesis, and membrane dynamics. To date, 13 different septin genes have been identified in mammals (SEPT1 to SEPT12 and SEPT14), which can be classified into four distinct subgroups based on the sequence homology of their domain structure (SEPT2, SEPT3, SEPT6, and SEPT7 subgroup). The family members of these subgroups have a strong affinity for other septins and form apolar tri-, hexa-, or octameric complexes consisting of multiple septin polypeptides...
2017: Frontiers in Cell and Developmental Biology
https://www.readbyqxmd.com/read/28223803/protein-nanocoatings-on-synthetic-polymeric-nanofibrous-membranes-designed-as-carriers-for-skin-cells
#19
Marketa Bacakova, Julia Pajorova, Denisa Stranska, Daniel Hadraba, Frantisek Lopot, Tomas Riedel, Eduard Brynda, Margit Zaloudkova, Lucie Bacakova
Protein-coated resorbable synthetic polymeric nanofibrous membranes are promising for the fabrication of advanced skin substitutes. We fabricated electrospun polylactic acid and poly(lactide-co-glycolic acid) nanofibrous membranes and coated them with fibrin or collagen I. Fibronectin was attached to a fibrin or collagen nanocoating, in order further to enhance the cell adhesion and spreading. Fibrin regularly formed a coating around individual nanofibers in the membranes, and also formed a thin noncontinuous nanofibrous mesh on top of the membranes...
2017: International Journal of Nanomedicine
https://www.readbyqxmd.com/read/28223522/conformational-dynamics-of-a-neurotransmitter-sodium-symporter-in-a-lipid-bilayer
#20
Suraj Adhikary, Daniel J Deredge, Anu Nagarajan, Lucy R Forrest, Patrick L Wintrode, Satinder K Singh
Neurotransmitter:sodium symporters (NSSs) are integral membrane proteins responsible for the sodium-dependent reuptake of small-molecule neurotransmitters from the synaptic cleft. The symporters for the biogenic amines serotonin (SERT), dopamine (DAT), and norepinephrine (NET) are targets of multiple psychoactive agents, and their dysfunction has been implicated in numerous neuropsychiatric ailments. LeuT, a thermostable eubacterial NSS homolog, has been exploited as a model protein for NSS members to canvass the conformational mechanism of transport with a combination of X-ray crystallography, cysteine accessibility, and solution spectroscopy...
February 21, 2017: Proceedings of the National Academy of Sciences of the United States of America
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