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3sch

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Co(II)-HppE with R-HPP

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Retrieved from "http://52.214.119.220/wiki/index.php/3sch"

Categories: Large Structures | Streptomyces wedmorensis | Drennan CL

@@ Line 3: / Line 3: @@
 <StructureSection load='3sch' size='340' side='right'caption='[[3sch]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sch]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_wedmorensis"_milard_and_burr_1926 "actinomyces wedmorensis" milard and burr 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SCH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SCH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=TB6:[(2R)-2-HYDROXYPROPYL]PHOSPHONIC+ACID'>TB6</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TB6:[(2R)-2-HYDROXYPROPYL]PHOSPHONIC+ACID'>TB6</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3scf|3scf]], [[3scg|3scg]]</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=3sch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sch OCA], [https://pdbe.org/3sch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sch RCSB], [https://www.ebi.ac.uk/pdbsum/3sch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sch ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fom4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43759 "Actinomyces wedmorensis" Milard and Burr 1926])</td></tr>
-<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=3sch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sch OCA], [http://pdbe.org/3sch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sch RCSB], [http://www.ebi.ac.uk/pdbsum/3sch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sch ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/HPPE_STRWE HPPE_STRWE] Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.<ref>PMID:16015285</ref> <ref>PMID:16186494</ref>
-Hydroxypropylphosphonic acid epoxidase (HppE) is an unusual mononuclear iron enzyme that uses dioxygen to catalyze the oxidative epoxidation of (S)-2-hydroxypropylphosphonic acid (S-HPP) in the biosynthesis of the antibiotic fosfomycin. Additionally, the enzyme converts the R-enantiomer of the substrate (R-HPP) to 2-oxo-propylphosphonic acid. To probe the mechanism of HppE regiospecificity, we determined three X-ray structures: R-HPP with inert cobalt-containing enzyme (Co(II)-HppE) at 2.1 A resolution; R-HPP with active iron-containing enzyme (Fe(II)-HppE) at 3.0 A resolution; and S-HPP-Fe(II)-HppE in complex with dioxygen mimic NO at 2.9 A resolution. These structures, along with previously determined structures of S-HPP-HppE, identify the dioxygen binding site on iron and elegantly illustrate how HppE is able to recognize both substrate enantiomers to catalyze two completely distinct reactions.
-Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis.,Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL J Am Chem Soc. 2011 Jun 30. PMID:21682308<ref>PMID:21682308</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3sch" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Actinomyces wedmorensis milard and burr 1926]]
 [[Category: Large Structures]]
-[[Category: Drennan, C L]]
+[[Category: Streptomyces wedmorensis]]
-[[Category: Cupin-fold]]
+[[Category: Drennan CL]]
-[[Category: Hydroxypropylphosphonic acid epoxidase]]
-[[Category: Metal binding protein]]
-[[Category: Mononuclear non-heme iron]]

3sch

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Co(II)-HppE with R-HPP

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