6o9a

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m (Protected "6o9a" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6o9a is ON HOLD
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==Crystal structure of MqnA complexed with 3-hydroxybenzoic acid==
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<StructureSection load='6o9a' size='340' side='right'caption='[[6o9a]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6o9a]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O9A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3HB:3-HYDROXYBENZOIC+ACID'>3HB</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_dehydratase Chorismate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.151 4.2.1.151] </span></td></tr>
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<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=6o9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o9a OCA], [http://pdbe.org/6o9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o9a RCSB], [http://www.ebi.ac.uk/pdbsum/6o9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o9a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/Q9RXE3_DEIRA Q9RXE3_DEIRA]] Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).[HAMAP-Rule:MF_00995]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Menaquinone (MK, vitamin K) is a lipid-soluble quinone that participates in the bacterial electron transport chain. In mammalian cells, vitamin K functions as an essential vitamin for the activation of several proteins involved in blood clotting and bone metabolism. MqnA is the first enzyme on the futalosine-dependent pathway to menaquinone and catalyzes the aromatization of chorismate by water loss. Here we report biochemical and structural studies of MqnA. These studies suggest that the dehydration reaction proceeds by a variant of the E1cb mechanism in which deprotonation is slower than water loss and that the enol carboxylate of the substrate is serving as the base.
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Authors: Hicks, K.A., Mahanta, N., Naseem, S., Fedoseyenko, D., Begley, T.P., Ealick, S.E.
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Menaquinone Biosynthesis: Biochemical and Structural Studies of Chorismate Dehydratase.,Mahanta N, Hicks KA, Naseem S, Zhang Y, Fedoseyenko D, Ealick SE, Begley TP Biochemistry. 2019 Mar 22. doi: 10.1021/acs.biochem.9b00105. PMID:30855131<ref>PMID:30855131</ref>
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Description: Crystal structure of MqnA complexed with 3-hydroxybenzoic acid
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Ealick, S.E]]
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<div class="pdbe-citations 6o9a" style="background-color:#fffaf0;"></div>
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[[Category: Begley, T.P]]
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== References ==
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[[Category: Hicks, K.A]]
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<references/>
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[[Category: Mahanta, N]]
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__TOC__
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</StructureSection>
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[[Category: Chorismate dehydratase]]
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[[Category: Large Structures]]
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[[Category: Begley, T P]]
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[[Category: Ealick, S E]]
[[Category: Fedoseyenko, D]]
[[Category: Fedoseyenko, D]]
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[[Category: Hicks, K A]]
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[[Category: Mahanta, N]]
[[Category: Naseem, S]]
[[Category: Naseem, S]]
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[[Category: Lyase]]
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[[Category: Menaquinone biosynthesis]]

Revision as of 07:12, 3 April 2019

Crystal structure of MqnA complexed with 3-hydroxybenzoic acid

PDB ID 6o9a

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