1tf0
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Crystal structure of the GA module complexed with human serum albumin
OverviewOverview
Many bactericide species express surface proteins that interact with human, serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia, magna (formerly Peptostreptococcus magnus) represents one of these, proteins. Protein PAB contains a domain of 53 amino acid residues known as, the GA module. GA homologs are also found in protein G of group C and G, streptococci. Here we report the crystal structure of HSA in complex with, the GA module of protein PAB. The model of the complex was refined to a, resolution of 2.7 A and reveals a novel binding epitope located in domain, II of the albumin molecule. The GA module is composed of a left-handed, three-helix bundle, and residues from the second helix and the loops, surrounding it were found to be involved in HSA binding. Furthermore, the, presence of HSA-bound fatty acids seems to influence HSA-GA complex, formation. F. magna has a much more restricted host specificity compared, with C and G streptococci, which is also reflected in the binding of, different animal albumins by proteins PAB and G. The structure of the, HSA-GA complex offers a molecular explanation to this unusually clear, example of bacterial adaptation.
DiseaseDisease
Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]
About this StructureAbout this Structure
1TF0 is a Protein complex structure of sequences from Finegoldia magna and Homo sapiens with DKA and CIT as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin., Lejon S, Frick IM, Bjorck L, Wikstrom M, Svensson S, J Biol Chem. 2004 Oct 8;279(41):42924-8. Epub 2004 Jul 21. PMID:15269208
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