Danielle E Fortune, Yi-Pin Lin, Ranjit K Deka, Ashley M Groshong, Brendan P Moore, Kayla E Hagman, John M Leong, Diana R Tomchick, Jon S Blevins
Decorin-binding protein A (DbpA) of Borrelia burgdorferi mediates bacterial adhesion to heparin and dermatan sulfate associated with decorin. Lysines K82, K163, and K170 of DbpA are known to be important for in vitro interaction with decorin, and the DbpA structure, initially solved by nuclear magnetic resonance (NMR) spectroscopy, suggests these lysine residues colocalize in a pocket near the C terminus of the protein. In the current study, we solved the structure of DbpA from B. burgdorferi strain 297 using X-ray crystallography and confirmed the existing NMR structural data...
August 2014: Infection and Immunity