2fp1: Difference between revisions
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==Secreted Chorismate Mutase from Mycobacterium tuberculosis== | ==Secreted Chorismate Mutase from Mycobacterium tuberculosis== | ||
<StructureSection load='2fp1' size='340' side='right' caption='[[2fp1]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='2fp1' size='340' side='right' caption='[[2fp1]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fp2|2fp2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fp2|2fp2]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fp1 OCA], [http://pdbe.org/2fp1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fp1 RCSB], [http://www.ebi.ac.uk/pdbsum/2fp1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fp1 OCA], [http://pdbe.org/2fp1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fp1 RCSB], [http://www.ebi.ac.uk/pdbsum/2fp1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fp1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/2fp1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/2fp1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:58, 14 June 2018
Secreted Chorismate Mutase from Mycobacterium tuberculosisSecreted Chorismate Mutase from Mycobacterium tuberculosis
Structural highlights
Function[SCMU_MYCTO] Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity (By similarity). 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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