3rzz

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<StructureSection load='3rzz' size='340' side='right'caption='[[3rzz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3rzz' size='340' side='right'caption='[[3rzz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rzz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_viridochromogenes"_krainsky_1914 "actinomyces viridochromogenes" krainsky 1914]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rzz]] 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=3RZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZZ 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=CD:CADMIUM+ION'>CD</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]] 2.2&#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;'>[[3gbf|3gbf]], [[3g7d|3g7d]]</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=CD:CADMIUM+ION'>CD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phpD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1938 "Actinomyces viridochromogenes" Krainsky 1914])</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=3rzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzz OCA], [https://pdbe.org/3rzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rzz RCSB], [https://www.ebi.ac.uk/pdbsum/3rzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzz 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=3rzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzz OCA], [https://pdbe.org/3rzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rzz RCSB], [https://www.ebi.ac.uk/pdbsum/3rzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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HEPD belongs to the superfamily of 2-His-1-carboxylate non-heme iron-dependent dioxygenases. It converts 2-hydroxyethylphosphonate (2-HEP) to hydroxymethylphosphonate (HMP) and formate. Previously postulated mechanisms for the reaction catalyzed by HEPD cannot explain its conversion of 1-HEP to acetylphosphate. Alternative mechanisms that involve either phosphite or methylphosphonate as intermediates, which potentially explain all experimental studies including isotope labeling experiments and use of substrate analogues, were investigated. The results of these studies reveal that these alternative mechanisms are not correct. Site-directed mutagenesis studies of Lys16, Arg90, and Tyr98 support roles of these residues in binding of 2-HEP. Mutation of Lys16 to Ala resulted in an inactive enzyme, whereas mutation of Arg90 to Ala or Tyr98 to Phe greatly decreased k(cat)/K(m,2-HEP). Furthermore, the latter mutants could not be saturated in O(2). These results suggest that proper binding of 2-HEP is important for O(2) activation and that the enzyme uses a compulsory binding order with 2-HEP binding before O(2). The Y98F mutant produces methylphosphonate as a minor side product providing indirect support for the proposal that the last step during catalysis involves a ferric hydroxide reacting with a methylphosphonate radical.
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Mechanism and Substrate Recognition of 2-Hydroxyethylphosphonate Dioxygenase.,Peck SC, Cooke HA, Cicchillo RM, Malova P, Hammerschmidt F, Nair SK, van der Donk WA Biochemistry. 2011 Jul 8. PMID:21711001<ref>PMID:21711001</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 3rzz" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Actinomyces viridochromogenes krainsky 1914]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cooke, H A]]
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[[Category: Streptomyces viridochromogenes]]
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[[Category: Biosynthetic protein]]
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[[Category: Cooke HA]]
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[[Category: Cupin]]
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[[Category: Oxidoreductase]]
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Current revision

Structure of Hydroxyethylphoshphonate Dioxygenase Y98F Mutant

PDB ID 3rzz

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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