2bu9
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(New page: 200px<br /> <applet load="2bu9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bu9, resolution 1.30Å" /> '''ISOPENICILLIN N SYN...)
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Revision as of 15:44, 29 October 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 [[1]], with EC number [1.21.3.1]. 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 Mon Oct 29 17:49:23 2007
