2au1
From Proteopedia
(New page: 200px<br /><applet load="2au1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2au1, resolution 2.4Å" /> '''Crystal Structure of ...) |
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==Overview== | ==Overview== | ||
| - | Group A Streptococcus secretes cysteine proteases named Mac-1 and Mac-2 | + | 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== | ==About this Structure== | ||
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[[Category: Agniswamy, J.]] | [[Category: Agniswamy, J.]] | ||
[[Category: Liu, M.]] | [[Category: Liu, M.]] | ||
| - | [[Category: Musser, J | + | [[Category: Musser, J M.]] |
| - | [[Category: Nagiec, M | + | [[Category: Nagiec, M J.]] |
[[Category: Schuck, P.]] | [[Category: Schuck, P.]] | ||
| - | [[Category: Sun, P | + | [[Category: Sun, P D.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: mac-1]] | [[Category: mac-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:00 2008'' |
Revision as of 14:31, 21 February 2008
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Crystal Structure of group A Streptococcus MAC-1 orthorhombic form
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
2AU1 is a Single protein structure of sequence from Streptococcus pyogenes mgas315 with as ligand. 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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