3sch: Difference between revisions
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==Co(II)-HppE with R-HPP== | ==Co(II)-HppE with R-HPP== | ||
<StructureSection load='3sch' size='340' side='right' caption='[[3sch]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3sch' size='340' side='right'caption='[[3sch]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == 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 [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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3sch" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3sch" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Epoxidase 3D structures|Epoxidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Actinomyces wedmorensis milard and burr 1926]] | [[Category: Actinomyces wedmorensis milard and burr 1926]] | ||
[[Category: Large Structures]] | |||
[[Category: Drennan, C L]] | [[Category: Drennan, C L]] | ||
[[Category: Cupin-fold]] | [[Category: Cupin-fold]] | ||
Revision as of 18:53, 20 November 2019
Co(II)-HppE with R-HPPCo(II)-HppE with R-HPP
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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