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2au1
From Proteopedia
Revision as of 02:14, 30 September 2014 by OCA (Talk | contribs)
2au1 is a 1 chain structure with sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Group A Streptococcus secretes cysteine proteases named Mac-1 and Mac-2 that mediate host immune evasion by targeting both IgG and Fc receptors. Here, we report the crystal structures of Mac-1 and its catalytically inactive C94A mutant in two different crystal forms. Despite the lack of sequence homology, Mac-1 adopts the canonical papain fold. Alanine mutations at the active site confirmed the critical residues involved in a papain-like catalytic mechanism. Mac-1 forms a symmetric dimer in both crystal forms and displays the unique dimer interface among papain superfamily members. Mutations at the dimer interface resulted in a significant reduction in IgG binding and catalysis, suggesting that the dimer contributes to both IgG specificity and enzyme cooperativity. A tunnel observed at the dimer interface constitutes a target for designing potential Mac-1-specific antimicrobial agents. The structures also offer insight into the functional difference between Mac-1 and Mac-2.
Crystal structure of group A streptococcus Mac-1: insight into dimer-mediated specificity for recognition of human IgG.,Agniswamy J, Nagiec MJ, Liu M, Schuck P, Musser JM, Sun PD Structure. 2006 Feb;14(2):225-35. PMID:16472742[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Agniswamy J, Nagiec MJ, Liu M, Schuck P, Musser JM, Sun PD. Crystal structure of group A streptococcus Mac-1: insight into dimer-mediated specificity for recognition of human IgG. Structure. 2006 Feb;14(2):225-35. PMID:16472742 doi:10.1016/j.str.2005.10.012
