3sch

Co(II)-HppE with R-HPPCo(II)-HppE with R-HPP

Structural highlights 3sch is a 2 chain structure with sequence from "actinomyces_wedmorensis"_milard_and_burr_1926 "actinomyces wedmorensis" milard and burr 1926. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , NonStd Res: Related: 3scf, 3scg Gene: fom4 ("Actinomyces wedmorensis" Milard and Burr 1926) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Epoxidase 3D structures

spinqualitylabelsall models 3sch, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image