2bu9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses | + | 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== | ==About this Structure== | ||
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[[Category: Isopenicillin-N synthase]] | [[Category: Isopenicillin-N synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adlington, R | + | [[Category: Adlington, R M.]] |
| - | [[Category: Baldwin, J | + | [[Category: Baldwin, J E.]] |
| - | [[Category: Clifton, I | + | [[Category: Clifton, I J.]] |
| - | [[Category: Howard-Jones, A | + | [[Category: Howard-Jones, A R.]] |
| - | [[Category: Rutledge, P | + | [[Category: Rutledge, P J.]] |
[[Category: FE]] | [[Category: FE]] | ||
[[Category: HFV]] | [[Category: HFV]] | ||
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:47 2008'' |
Revision as of 14:41, 21 February 2008
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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 , and as ligands. Active as Isopenicillin-N synthase, with EC number 1.21.3.1 Known structural/functional Site: . 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 Thu Feb 21 16:41:47 2008
