1uzw
From Proteopedia
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ISOPENICILLIN N SYNTHASE WITH L-D-(A-AMINOADIPOYL)-L-CYSTEINYL-D-ISODEHYDROVALINE
Overview
Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses, the formation of bicyclic isopenicillin N from, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV). In this study we, report a novel activity for the iron of the IPNS active site, which, behaves as a Lewis acid to catalyse the elimination of HF from the, fluorinated substrate analogue, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-beta-fluorovaline (ACbetaFV)., X-Ray crystallographic studies of IPNS crystals grown anaerobically with, ACbetaFV reveal that the valinyl beta-fluorine is missing from the active, site region, and suggest the presence of the unsaturated tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-isodehydrovaline in place of, substrate ACbetaFV. (19)F NMR studies confirm the release of ... [(full description)]
About this Structure
1UZW is a [Single protein] structure of sequence from [Emericella nidulans] with FE2, SO4 and CDH as [ligands]. Active as [[1]], with EC number [1.21.3.1]. Full crystallographic information is available from [OCA].
Reference
Active-site-mediated elimination of hydrogen fluoride from a fluorinated substrate analogue by isopenicillin N synthase., Grummitt AR, Rutledge PJ, Clifton IJ, Baldwin JE, Biochem J. 2004 Sep 1;382(Pt 2):659-66. PMID:15175003
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