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4yar

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'''Unreleased structure'''
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==2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H==
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<StructureSection load='4yar' size='340' side='right' caption='[[4yar]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4yar]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YAR 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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/2-hydroxyethylphosphonate_dioxygenase 2-hydroxyethylphosphonate dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.72 1.13.11.72] </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=4yar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yar OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yar RCSB], [http://www.ebi.ac.uk/pdbsum/4yar PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HEPD_STRVR HEPD_STRVR]] Non-heme-dependent dioxygenase that catalyzes the conversion of 2-hydroxyethylphosphonate (HEP) to hydroxymethylphosphonate (HMP) in the biosynthesis of phosphinothricin tripeptide (PTT). PTT contains the unusual amino acid phosphinothricin attached to 2 alanine residues. Synthetic phosphinothricin (glufosinate) is a key component of commercial herbicides.<ref>PMID:17632514</ref> <ref>PMID:19516340</ref> <ref>PMID:19839620</ref> <ref>PMID:21381767</ref> <ref>PMID:21711001</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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2-Hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS) are nonheme iron oxygenases that both catalyze the carbon-carbon bond cleavage of 2-hydroxyethylphosphonate but generate different products. Substrate labeling experiments led to a mechanistic hypothesis in which the fate of a common intermediate determined product identity. We report here the generation of a bifunctional mutant of HEPD (E176H) that exhibits the activity of both HEPD and MPnS. The product distribution of the mutant is sensitive to a substrate isotope effect, consistent with an isotope-sensitive branching mechanism involving a common intermediate. The X-ray structure of the mutant was determined and suggested that the introduced histidine does not coordinate the active site metal, unlike the iron-binding glutamate it replaced.
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The entry 4yar is ON HOLD until Paper Publication
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A Common Late-Stage Intermediate in Catalysis by 2-Hydroxyethyl-phosphonate Dioxygenase and Methylphosphonate Synthase.,Peck SC, Chekan JR, Ulrich EC, Nair SK, van der Donk WA J Am Chem Soc. 2015 Feb 26. PMID:25699631<ref>PMID:25699631</ref>
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Authors: Chekan, J.R., Nair, S.K.
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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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Description: 2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Nair, S.K]]
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__TOC__
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[[Category: Chekan, J.R]]
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</StructureSection>
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[[Category: 2-hydroxyethylphosphonate dioxygenase]]
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[[Category: Chekan, J R]]
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[[Category: Nair, S K]]
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[[Category: Dioxygenase]]

Revision as of 11:21, 4 March 2015

2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H

4yar, resolution 1.75Å

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