2bno: Difference between revisions

Revision as of 21:59, 27 July 2008

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File:2bno.png

Template:STRUCTURE 2bno

STRUCTURE OF A ZN ENZYMESTRUCTURE OF A ZN ENZYME

Template:ABSTRACT PUBMED 16186494

About this StructureAbout this Structure

2BNO is a Single protein structure of sequence from Streptomyces wedmorensis. 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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OCA

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 {{STRUCTURE_2bno|  PDB=2bno  |  SCENE=  }}
-'''STRUCTURE OF A ZN ENZYME'''
+===STRUCTURE OF A ZN ENZYME===
-==Overview==
+<!--
-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 catalytic center driven by the presence or absence of ligand, that HPPE is a Zn(2+)/Fe(2+)-dependent epoxidase, proof that flavin mononucleotide is required for catalysis, and allow us to propose a simple mechanism that is compatible with previous experimental data. The participation of the redox inert Zn(2+) in the mechanism is surprising and indicates that Lewis acid properties of the metal ions are sufficient to polarize the substrate and, aided by flavin mononucleotide reduction, facilitate the epoxidation.
+The line below this paragraph, {{ABSTRACT_PUBMED_16186494}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16186494 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16186494}}
 ==About this Structure==
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 [[Category: Epoxidase,cupin,hth,cation-dependant,zinc,fosfomycin]]
 [[Category: Oxidoreductase]]
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