2avw

From Proteopedia

---

Revision as of 16:11, 29 January 2008

proteopedia linkproteopedia link

spinqualitylabelsall models 2avw, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of monoclinic form of streptococcus Mac-1

Overview

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.

About this Structure

2AVW is a Single protein structure of sequence from Streptococcus pyogenes mgas315 with and as ligands. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jan 29 18:11:01 2008