2bno: Difference between revisions
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Revision as of 17:38, 30 October 2007
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STRUCTURE OF A ZN ENZYME
OverviewOverview
The biosynthesis of fosfomycin, an oxirane antibiotic in clinical use, involves a unique epoxidation catalyzed by (S)-2-hydroxypropylphosphonic, acid epoxidase (HPPE). The reaction is essentially dehydrogenation of a, secondary alcohol. A high-resolution crystallographic analysis reveals, that the HPPE subunit displays a two-domain combination. The C-terminal or, catalytic domain has the cupin fold that binds a divalent cation, whereas, the N-terminal domain carries a helix-turn-helix motif with putative, DNA-binding helices positioned 34 A apart. The structure of HPPE serves as, a model for numerous proteins, of ill-defined function, predicted to be, transcription factors but carrying a cupin domain at the C terminus., Structure-reactivity analyses reveal conformational changes near the, ... [(full description)]
About this StructureAbout this Structure
2BNO is a [Single protein] structure of sequence from [Streptomyces wedmorensis] with HG, ZN and SO4 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism., McLuskey K, Cameron S, Hammerschmidt F, Hunter WN, Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14221-6. Epub 2005 Sep 26. PMID:16186494
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