View source for 4yar


==2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H==
<StructureSection load='4yar' size='340' side='right'caption='[[4yar]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yar]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4YAR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yar OCA], [https://pdbe.org/4yar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yar RCSB], [https://www.ebi.ac.uk/pdbsum/4yar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yar ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HEPD_STRVT HEPD_STRVT] 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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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4yar" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces viridochromogenes]]
[[Category: Chekan JR]]
[[Category: Nair SK]]