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| - | [[Image:3g7d.png|left|200px]] | |
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| - | <!-- | + | ==Native PhpD with Cadmium Atoms== |
| - | The line below this paragraph, containing "STRUCTURE_3g7d", creates the "Structure Box" on the page.
| + | <StructureSection load='3g7d' size='340' side='right'caption='[[3g7d]], [[Resolution|resolution]] 1.80Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3g7d]] 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=3G7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G7D FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display. | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | {{STRUCTURE_3g7d| PDB=3g7d | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3g7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7d OCA], [https://pdbe.org/3g7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g7d RCSB], [https://www.ebi.ac.uk/pdbsum/3g7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7d 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> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Natural products containing phosphorus-carbon bonds have found widespread use in medicine and agriculture. One such compound, phosphinothricin tripeptide, contains the unusual amino acid phosphinothricin attached to two alanine residues. Synthetic phosphinothricin (glufosinate) is a component of two top-selling herbicides (Basta and Liberty), and is widely used with resistant transgenic crops including corn, cotton and canola. Recent genetic and biochemical studies showed that during phosphinothricin tripeptide biosynthesis 2-hydroxyethylphosphonate (HEP) is converted to hydroxymethylphosphonate (HMP). Here we report the in vitro reconstitution of this unprecedented C(sp(3))-C(sp(3)) bond cleavage reaction and X-ray crystal structures of the enzyme. The protein is a mononuclear non-haem iron(ii)-dependent dioxygenase that converts HEP to HMP and formate. In contrast to most other members of this family, the oxidative consumption of HEP does not require additional cofactors or the input of exogenous electrons. The current study expands the scope of reactions catalysed by the 2-His-1-carboxylate mononuclear non-haem iron family of enzymes. |
| | | | |
| - | ===Native PhpD with Cadmium Atoms===
| + | An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis.,Cicchillo RM, Zhang H, Blodgett JA, Whitteck JT, Li G, Nair SK, van der Donk WA, Metcalf WW Nature. 2009 Jun 11;459(7248):871-4. PMID:19516340<ref>PMID:19516340</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 3g7d" style="background-color:#fffaf0;"></div> |
| | | | |
| - | <!--
| + | ==See Also== |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_19516340}}, adds the Publication Abstract to the page
| + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 19516340 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_19516340}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Large Structures]] |
| - | [[3g7d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7D OCA]. | + | |
| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:019516340</ref><references group="xtra"/> | + | |
| | [[Category: Streptomyces viridochromogenes]] | | [[Category: Streptomyces viridochromogenes]] |
| - | [[Category: Nair, S K.]] | + | [[Category: Nair SK]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Cupin]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Natural products containing phosphorus-carbon bonds have found widespread use in medicine and agriculture. One such compound, phosphinothricin tripeptide, contains the unusual amino acid phosphinothricin attached to two alanine residues. Synthetic phosphinothricin (glufosinate) is a component of two top-selling herbicides (Basta and Liberty), and is widely used with resistant transgenic crops including corn, cotton and canola. Recent genetic and biochemical studies showed that during phosphinothricin tripeptide biosynthesis 2-hydroxyethylphosphonate (HEP) is converted to hydroxymethylphosphonate (HMP). Here we report the in vitro reconstitution of this unprecedented C(sp(3))-C(sp(3)) bond cleavage reaction and X-ray crystal structures of the enzyme. The protein is a mononuclear non-haem iron(ii)-dependent dioxygenase that converts HEP to HMP and formate. In contrast to most other members of this family, the oxidative consumption of HEP does not require additional cofactors or the input of exogenous electrons. The current study expands the scope of reactions catalysed by the 2-His-1-carboxylate mononuclear non-haem iron family of enzymes.
An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis.,Cicchillo RM, Zhang H, Blodgett JA, Whitteck JT, Li G, Nair SK, van der Donk WA, Metcalf WW Nature. 2009 Jun 11;459(7248):871-4. PMID:19516340[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blodgett JA, Thomas PM, Li G, Velasquez JE, van der Donk WA, Kelleher NL, Metcalf WW. Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide. Nat Chem Biol. 2007 Aug;3(8):480-5. Epub 2007 Jul 15. PMID:17632514 doi:http://dx.doi.org/10.1038/nchembio.2007.9
- ↑ Cicchillo RM, Zhang H, Blodgett JA, Whitteck JT, Li G, Nair SK, van der Donk WA, Metcalf WW. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature. 2009 Jun 11;459(7248):871-4. PMID:19516340 doi:10.1038/nature07972
- ↑ Whitteck JT, Cicchillo RM, van der Donk WA. Hydroperoxylation by hydroxyethylphosphonate dioxygenase. J Am Chem Soc. 2009 Nov 11;131(44):16225-32. doi: 10.1021/ja906238r. PMID:19839620 doi:http://dx.doi.org/10.1021/ja906238r
- ↑ Whitteck JT, Malova P, Peck SC, Cicchillo RM, Hammerschmidt F, van der Donk WA. On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase. J Am Chem Soc. 2011 Mar 30;133(12):4236-9. doi: 10.1021/ja1113326. Epub 2011 Mar , 7. PMID:21381767 doi:http://dx.doi.org/10.1021/ja1113326
- ↑ Peck SC, Cooke HA, Cicchillo RM, Malova P, Hammerschmidt F, Nair SK, van der Donk WA. Mechanism and Substrate Recognition of 2-Hydroxyethylphosphonate Dioxygenase. Biochemistry. 2011 Jul 8. PMID:21711001 doi:10.1021/bi200804r
- ↑ Cicchillo RM, Zhang H, Blodgett JA, Whitteck JT, Li G, Nair SK, van der Donk WA, Metcalf WW. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature. 2009 Jun 11;459(7248):871-4. PMID:19516340 doi:10.1038/nature07972
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