3sch: Difference between revisions
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==Co(II)-HppE with R-HPP== | |||
<StructureSection load='3sch' size='340' side='right'caption='[[3sch]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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='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> | |||
</table> | |||
== Function == | |||
[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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3sch" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Epoxidase 3D structures|Epoxidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces wedmorensis]] | |||
[[Category: Drennan CL]] | |||
Latest revision as of 05:23, 21 November 2024
Co(II)-HppE with R-HPPCo(II)-HppE with R-HPP
Structural highlights
FunctionHPPE_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.[1] [2] Publication Abstract from PubMedHydroxypropylphosphonic 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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