2AVW

Crystal structure of monoclinic form of streptococcus Mac-1

2AVW の概要

• エントリーDOI: 10.2210/pdb2avw/pdb
• 分子名称: IgG-degrading protease, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: mac-1, hydrolase
• 由来する生物種: Streptococcus pyogenes
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 211179.38

構造登録者

Agniswamy, J.,Nagiec, M.J.,Liu, M.,Schuck, P.,Musser, J.M.,Sun, P.D. (登録日: 2005-08-30, 公開日: 2006-02-28, 最終更新日: 2024-02-14)

主引用文献

Agniswamy, J.,Nagiec, M.J.,Liu, M.,Schuck, P.,Musser, J.M.,Sun, P.D.
Crystal structure of group a streptococcus mac-1: insight into dimer-mediated specificity for recognition of human IgG.
Structure, 14:225-235, 2006

PubMed Abstract: 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.

PubMed: 16472742
DOI: 10.1016/j.str.2005.10.012

実験手法

X-RAY DIFFRACTION (2 Å)