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2eua
From Proteopedia
(Difference between revisions)
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<StructureSection load='2eua' size='340' side='right'caption='[[2eua]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2eua' size='340' side='right'caption='[[2eua]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2eua]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2eua]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EUA FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr> | |
| - | <tr id=' | + | |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eua OCA], [https://pdbe.org/2eua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eua RCSB], [https://www.ebi.ac.uk/pdbsum/2eua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eua 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=2eua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eua OCA], [https://pdbe.org/2eua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eua RCSB], [https://www.ebi.ac.uk/pdbsum/2eua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eua ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MENF_ECOLI MENF_ECOLI] | ||
== 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=2eua 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=2eua ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Menaquinone biosynthesis is initiated by the conversion of chorismate to isochorismate, a reaction that is catalyzed by the menaquinone-specific isochorismate synthase, MenF. The catalytic mechanism of MenF has been probed using a combination of structural and biochemical studies, including the 2.5 A structure of the enzyme, and Lys190 has been identified as the base that activates water for nucleophilic attack at the chorismate C2 carbon. MenF is a member of a larger family of Mg2+ dependent chorismate binding enzymes catalyzing distinct chorismate transformations. The studies reported here extend the mechanism recently proposed for this enzyme family by He et al.: He, Z., Stigers Lavoie, K. D., Bartlett, P. A., and Toney, M. D. (2004) J. Am. Chem. Soc. 126, 2378-85. | ||
| - | |||
| - | Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family.,Kolappan S, Zwahlen J, Zhou R, Truglio JJ, Tonge PJ, Kisker C Biochemistry. 2007 Jan 30;46(4):946-53. PMID:17240978<ref>PMID:17240978</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2eua" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kisker | + | [[Category: Kisker C]] |
| - | [[Category: Kolappan | + | [[Category: Kolappan S]] |
| - | [[Category: Tonge | + | [[Category: Tonge PJ]] |
| - | [[Category: Zhou | + | [[Category: Zhou R]] |
| - | [[Category: Zwahlen | + | [[Category: Zwahlen J]] |
| - | + | ||
| - | + | ||
Current revision
Structure and Mechanism of MenF, the Menaquinone-Specific Isochorismate Synthase from Escherichia Coli
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