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==Secreted Chorismate Mutase from Mycobacterium tuberculosis== | |||
<StructureSection load='2fp2' size='340' side='right'caption='[[2fp2]], [[Resolution|resolution]] 1.64Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FP2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64Å</td></tr> | |||
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</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=2fp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fp2 OCA], [https://pdbe.org/2fp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fp2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fp2 ProSAT], [https://www.topsan.org/Proteins/TBSGC/2fp2 TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SCMU_MYCTU SCMU_MYCTU] Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.<ref>PMID:15654876</ref> <ref>PMID:15737998</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/2fp2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2fp2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The presence of exported chorismate mutases produced by certain organisms such as Mycobacterium tuberculosis has been shown to correlate with their pathogenicity. As such, these proteins comprise a new group of promising selective drug targets. Here, we report the high-resolution crystal structure of the secreted dimeric chorismate mutase from M. tuberculosis (*MtCM; encoded by Rv1885c), which represents the first 3D-structure of a member of this chorismate mutase family, termed the AroQ(gamma) subclass. Structures are presented both for the unliganded enzyme and for a complex with a transition state analog. The protomer fold resembles the structurally characterized (dimeric) Escherichia coli chorismate mutase domain, but exhibits a new topology, with helix H4 of *MtCM carrying the catalytic site residue missing in the shortened helix H1. Furthermore, the structure of each *MtCM protomer is significantly more compact and only harbors one active site pocket, which is formed entirely by one polypeptide chain. Apart from the structural model, we present evidence as to how the substrate may enter the active site. | |||
1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed.,Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U J Mol Biol. 2006 Apr 14;357(5):1483-99. Epub 2006 Feb 6. PMID:16499927<ref>PMID:16499927</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2fp2" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]] | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: | |||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Dey R]] | |||
[[Category: Dey | [[Category: Grahn E]] | ||
[[Category: Grahn | [[Category: Kast P]] | ||
[[Category: Kast | [[Category: Krengel U]] | ||
[[Category: Krengel | [[Category: Okvist M]] | ||
[[Category: Okvist | [[Category: Sasso S]] | ||
[[Category: Sasso | |||
Latest revision as of 11:00, 30 October 2024
Secreted Chorismate Mutase from Mycobacterium tuberculosisSecreted Chorismate Mutase from Mycobacterium tuberculosis
Structural highlights
FunctionSCMU_MYCTU Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe presence of exported chorismate mutases produced by certain organisms such as Mycobacterium tuberculosis has been shown to correlate with their pathogenicity. As such, these proteins comprise a new group of promising selective drug targets. Here, we report the high-resolution crystal structure of the secreted dimeric chorismate mutase from M. tuberculosis (*MtCM; encoded by Rv1885c), which represents the first 3D-structure of a member of this chorismate mutase family, termed the AroQ(gamma) subclass. Structures are presented both for the unliganded enzyme and for a complex with a transition state analog. The protomer fold resembles the structurally characterized (dimeric) Escherichia coli chorismate mutase domain, but exhibits a new topology, with helix H4 of *MtCM carrying the catalytic site residue missing in the shortened helix H1. Furthermore, the structure of each *MtCM protomer is significantly more compact and only harbors one active site pocket, which is formed entirely by one polypeptide chain. Apart from the structural model, we present evidence as to how the substrate may enter the active site. 1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed.,Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U J Mol Biol. 2006 Apr 14;357(5):1483-99. Epub 2006 Feb 6. PMID:16499927[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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