Crystal structure of a bacterial albumin-binding domain at 1.4
Å resolution
Abstract
The albumin-binding domain, or GA module, of the peptostreptococcal albumin-binding protein expressed in pathogenic strains of Finegoldia magna is believed to be responsible for the virulence and increased growth rate of these strains. Here we present the 1.4
Å crystal structure of this domain, and compare it with the crystal structure of the GA–albumin complex. An analysis of protein–protein interactions in the two crystals, and the presence of multimeric GA species in solution, indicate the GA module is “sticky”, and is capable of forming contacts with a range of protein surfaces. This might lead to interactions with different host proteins.
Abbreviations: HSA, human serum albumin, GA, protein G-like albumin-binding, NMR, nuclear magnetic resonance, rms, root mean square
Keywords: GA module, Peptostreptococcal albumin-binding protein, Human serum albumin, Bacterial mimicry, X-ray crystallography
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PII: S0014-5793(07)00650-3
doi:10.1016/j.febslet.2007.06.003
© 2007 Federation of European Biochemical Societies
