2bu9
From Proteopedia
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
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Revision as of 15:43, 5 November 2007
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ISOPENICILLIN N SYNTHASE COMPLEXED WITH L-AMINOADIPOYL-L-CYSTEINYL-L-HEXAFLUOROVALINE
Overview
Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses, the formation of isopenicillin N from the tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine. In this report, we, describe the crystal structure of the enzyme with a non-natural, L,L,L-tripeptide substrate, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-L-3,3,3,3',3',3'-hexafluorovaline, . This structure reveals a strong binding interaction of the tripeptide, within the active site and a unique conformation for the non-natural, L,L,L-diastereomer. Taken together, these findings provide a possible, rationale for the previously observed inhibitory effects of, L,L,L-tripeptide substrates on IPNS activity.
About this Structure
2BU9 is a Single protein structure of sequence from Emericella nidulans with FE, SO4 and HFV as ligands. Active as Isopenicillin-N synthase, with EC number 1.21.3.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Unique binding of a non-natural L,L,L-substrate by isopenicillin N synthase., Howard-Jones AR, Rutledge PJ, Clifton IJ, Adlington RM, Baldwin JE, Biochem Biophys Res Commun. 2005 Oct 21;336(2):702-8. PMID:16143309
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