2bu9: Difference between revisions
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'''ISOPENICILLIN N SYNTHASE COMPLEXED WITH L-AMINOADIPOYL-L-CYSTEINYL-L-HEXAFLUOROVALINE''' | '''ISOPENICILLIN N SYNTHASE COMPLEXED WITH L-AMINOADIPOYL-L-CYSTEINYL-L-HEXAFLUOROVALINE''' | ||
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[[Category: Howard-Jones, A R.]] | [[Category: Howard-Jones, A R.]] | ||
[[Category: Rutledge, P J.]] | [[Category: Rutledge, P J.]] | ||
[[Category: | [[Category: Antibiotic biosynthesis]] | ||
[[Category: | [[Category: B-lactam antibiotic]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Oxygenase]] | ||
[[Category: | [[Category: Penicillin biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:48:25 2008'' | |||
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Revision as of 17:48, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 20:48:25 2008
