1tf0: Difference between revisions

Revision as of 05:20, 29 July 2008

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File:1tf0.png

Template:STRUCTURE 1tf0

Crystal structure of the GA module complexed with human serum albuminCrystal structure of the GA module complexed with human serum albumin

Template:ABSTRACT PUBMED 15269208

About this StructureAbout this Structure

1TF0 is a Protein complex structure of sequences from Finegoldia magna and Homo sapiens. 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

Page seeded by OCA on Tue Jul 29 05:20:40 2008

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OCA

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-'''Crystal structure of the GA module complexed with human serum albumin'''
+===Crystal structure of the GA module complexed with human serum albumin===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15269208}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15269208}}
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 [[Category: Wikstrom, M.]]
 [[Category: Protein-protein complex]]
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