2avw

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spinqualitylabelsall models PDB ID 2avw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.0Å
Ligands:	and
Gene:	mac (Streptococcus pyogenes MGAS315)
Coordinates:	save as pdb, mmCIF, xml

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. 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

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