2au1: Difference between revisions

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<StructureSection load='2au1' size='340' side='right'caption='[[2au1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2au1' size='340' side='right'caption='[[2au1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2au1]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2AU1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2au1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_MGAS5005 Streptococcus pyogenes MGAS5005]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2AU1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2au1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2au1 OCA], [https://pdbe.org/2au1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2au1 RCSB], [https://www.ebi.ac.uk/pdbsum/2au1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2au1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2au1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2au1 OCA], [https://pdbe.org/2au1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2au1 RCSB], [https://www.ebi.ac.uk/pdbsum/2au1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2au1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7DAM2_STRP1 Q7DAM2_STRP1]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=2au1 ConSurf].
</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/main_output.php?pdb_ID=2au1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2au1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes MGAS5005]]
[[Category: Agniswamy, J]]
[[Category: Agniswamy J]]
[[Category: Liu, M]]
[[Category: Liu M]]
[[Category: Musser, J M]]
[[Category: Musser JM]]
[[Category: Nagiec, M J]]
[[Category: Nagiec MJ]]
[[Category: Schuck, P]]
[[Category: Schuck P]]
[[Category: Sun, P D]]
[[Category: Sun PD]]
[[Category: Hydrolase]]
[[Category: Mac-1]]

Latest revision as of 09:14, 14 February 2024

Crystal Structure of group A Streptococcus MAC-1 orthorhombic form

2au1, resolution 2.40Å

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