3scf

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[[Image:3scf.png|left|200px]]
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==Fe(II)-HppE with S-HPP and NO==
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<StructureSection load='3scf' size='340' side='right' caption='[[3scf]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3scf]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SCF FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=S0H:(S)-2-HYDROXYPROPYLPHOSPHONIC+ACID'>S0H</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3scg|3scg]], [[3sch|3sch]]</td></tr>
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<tr><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 Streptomyces wedmorensis])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3scf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3scf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3scf RCSB], [http://www.ebi.ac.uk/pdbsum/3scf PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_3scf", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3scf| PDB=3scf | SCENE= }}
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===Fe(II)-HppE with S-HPP and NO===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21682308}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 21682308 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_21682308}}
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==About this Structure==
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[[3scf]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SCF OCA].
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==Reference==
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<ref group="xtra">PMID:021682308</ref><references group="xtra"/>
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[[Category: Streptomyces wedmorensis]]
[[Category: Streptomyces wedmorensis]]
[[Category: Drennan, C L.]]
[[Category: Drennan, C L.]]

Revision as of 05:25, 5 June 2014

Fe(II)-HppE with S-HPP and NO

3scf, resolution 2.85Å

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