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2au1

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[[Image:2au1.png|left|200px]]
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==Crystal Structure of group A Streptococcus MAC-1 orthorhombic form==
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<StructureSection load='2au1' size='340' side='right' caption='[[2au1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2au1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AU1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2au1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2au1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2au1 RCSB], [http://www.ebi.ac.uk/pdbsum/2au1 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/2au1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2au1| PDB=2au1 | SCENE= }}
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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<ref>PMID:16472742</ref>
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===Crystal Structure of group A Streptococcus MAC-1 orthorhombic form===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_16472742}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2au1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AU1 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:016472742</ref><references group="xtra"/>
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[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
[[Category: Agniswamy, J.]]
[[Category: Agniswamy, J.]]

Revision as of 02:14, 30 September 2014

Crystal Structure of group A Streptococcus MAC-1 orthorhombic form

2au1, resolution 2.40Å

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