1w3x: Difference between revisions

Revision as of 19:34, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1w3x.png

Template:STRUCTURE 1w3x

ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL)-(3R)-METHYL-L-CYSTEINE D-A-HYDROXYISOVALERYL ESTER COMPLEX (OXYGEN EXPOSED 5 MINUTES 20 BAR)ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL)-(3R)-METHYL-L-CYSTEINE D-A-HYDROXYISOVALERYL ESTER COMPLEX (OXYGEN EXPOSED 5 MINUTES 20 BAR)

Template:ABSTRACT PUBMED 16444759

About this StructureAbout this Structure

1W3X is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.

ReferenceReference

Unexpected oxidation of a depsipeptide substrate analogue in crystalline isopenicillin N synthase., Daruzzaman A, Clifton IJ, Adlington RM, Baldwin JE, Rutledge PJ, Chembiochem. 2006 Feb;7(2):351-8. PMID:16444759

Page seeded by OCA on Mon Jul 28 19:34:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1w3x.gif|left|200px]]
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 {{STRUCTURE_1w3x|  PDB=1w3x  |  SCENE=  }}
-'''ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL)-(3R)-METHYL-L-CYSTEINE D-A-HYDROXYISOVALERYL ESTER COMPLEX (OXYGEN EXPOSED 5 MINUTES 20 BAR)'''
+===ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL)-(3R)-METHYL-L-CYSTEINE D-A-HYDROXYISOVALERYL ESTER COMPLEX (OXYGEN EXPOSED 5 MINUTES 20 BAR)===
-==Overview==
+<!--
-Isopenicillin N synthase (IPNS) is a non-heme iron(ii)-dependent oxidase that is central to penicillin biosynthesis. Herein, we report mechanistic studies of the IPNS reaction in the crystalline state, using the substrate analogue delta-(L-alpha-aminoadipoyl)-(3R)-methyl-L-cysteine D-alpha-hydroxyisovaleryl ester (AmCOV) to probe the early stages of the catalytic cycle. The X-ray crystal structure of the anaerobic IPNS:Fe(II):AmCOV complex was solved to 1.40 A resolution, and it reveals several subtle differences in the active site relative to the complex of the enzyme with its natural substrate. The crystalline IPNS:Fe(II):AmCOV complex was then exposed to oxygen gas at high pressure; this brought about reaction to give what appears to be a hydroxymethyl/ene-thiol product. A mechanism for this reaction is proposed. These results offer further insight into the delicate interplay of steric and electronic effects in the IPNS active site and the mechanistic intricacies of this remarkable enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_16444759}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16444759 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16444759}}
 ==About this Structure==
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 [[Category: Oxygenase]]
 [[Category: Penicillin biosynthesis]]
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