2wo7 | pdb_00002wo7

Isopenicillin N synthase with substrate analogue L,L,D-ACd2Ab (unexposed)

spinqualitylabelsall models 2wo7, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wo7 is a 1 chain structure with sequence from A. nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ASV, FE2 Related: 1hb4, 1blz, 1oc1, 1w3v, 1uzw, 1ips, 1bk0, 1w3x, 2vbp, 1hb3, 1w04, 1qiq, 1qjf, 2bu9, 1obn, 1odm, 2vbd, 2vcm, 1odn, 1hb2, 2ve1, 2vau, 1qje, 1w03, 2vbb, 1w06, 2ivj, 1hb1, 2jb4, 1w05, 2ivi, 2bjs Activity: Isopenicillin-N synthase, with EC number 1.21.3.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IPNS_EMENI] Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Isopenicillin N synthase (IPNS) is a non-heme iron(II) oxidase which catalyses the biosynthesis of isopenicillin N (IPN) from the tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-valine (lld-ACV). Herein we report crystallographic studies to investigate the binding of a truncated lll-substrate in the active site of IPNS. Two epimeric tripeptides have been prepared by solution phase peptide synthesis and crystallised with the enzyme. delta-l-alpha-Aminoadipoyl-l-cysteinyl-d-2-amino-3,3-dideuteriobutyrate (lld-ACd(2)Ab) has the same configuration as the natural substrate lld-ACV at each of its three stereocentres; its epimer delta-l-alpha-aminoadipoyl-l-cysteinyl-l-2-amino-3,3-dideuteriobutyrate (lll-ACd(2)Ab) has the opposite configuration at its third amino acid. lll-ACV has previously been shown to inhibit IPNS turnover of its substrate lld-ACV; the all-protiated tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-2-aminobutyrate (lld-ACAb) is a substrate for IPNS, being turned over to a mixture of penam and cepham products. Comparisons between the crystal structures of the IPNS:Fe(II):lld-ACd(2)Ab and IPNS:Fe(II):lll-ACd(2)Ab complexes offer a possible rationale for the previously observed inhibitory effects of lll-ACV on IPNS activity. Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase.,Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ Biochem Biophys Res Commun. 2010 Aug 6;398(4):659-64. Epub 2010 Jul 13. PMID:20603104 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isopenicillin N synthase

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