3bzm

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3bzm]] is a 1 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=3BZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BZM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3bzm]] is a 1 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=3BZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BZM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bzn|3bzn]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">menF, yfbA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Isochorismate_synthase Isochorismate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.4.2 5.4.4.2] </span></td></tr>
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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=3bzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bzm OCA], [https://pdbe.org/3bzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bzm RCSB], [https://www.ebi.ac.uk/pdbsum/3bzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bzm 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=3bzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bzm OCA], [https://pdbe.org/3bzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bzm RCSB], [https://www.ebi.ac.uk/pdbsum/3bzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bzm ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[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=3bzm 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=3bzm ConSurf].
<div style="clear:both"></div>
<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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The electron carrier menaquinone is one of many important bacterial metabolites that are derived from the key intermediate chorismic acid. MenF, the first enzyme in the menaquinone pathway, catalyzes the isomerization of chorismate to isochorismate. Here, an improved structure of MenF in a new crystal form is presented. The structure, solved at 2.0 angstroms resolution in complex with magnesium, reveals a well defined closed active site. Existing evidence suggests that the mechanism of the reaction catalyzed by MenF involves nucleophilic attack of a water molecule on the chorismate ring. The structure reveals a well defined water molecule located in an appropriate position for activation by Lys190 and attack on the substrate.
 
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Structure of isochorismate synthase in complex with magnesium.,Parsons JF, Shi KM, Ladner JE Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):607-10. Epub 2008, Apr 19. PMID:18453696<ref>PMID:18453696</ref>
 
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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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<div class="pdbe-citations 3bzm" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Isochorismate synthase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ladner, J E]]
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[[Category: Ladner JE]]
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[[Category: Parsons, J F]]
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[[Category: Parsons JF]]
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[[Category: Shi, K M]]
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[[Category: Shi KM]]
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[[Category: Chorismate]]
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[[Category: Isochorismate]]
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[[Category: Isomerase]]
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[[Category: Menaquinone]]
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[[Category: Menaquinone biosynthesis]]
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Current revision

Crystal Structure of Open form of Menaquinone-Specific Isochorismate Synthase, MenF

PDB ID 3bzm

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