2vbd | pdb_00002vbd

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

spinqualitylabelsall models 2vbd, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vbd 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: FE2, V10 Related: 1hb1, 1ips, 1oc1, 1w04, 1w05, 1w3v, 2bjs, 2jb4, 2vau, 1bk0, 1blz, 1hb2, 1hb3, 1hb4, 1obn, 1odm, 1odn, 1qiq, 1qje, 1qjf, 1uzw, 1w03, 1w06, 1w3x, 2bu9, 2ivi, 2ivj, 2vbb 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) in a remarkable oxidative bicyclisation reaction. The natural substrate for IPNS is the lld-configured tripeptide. lll-ACV is not turned over by the enzyme, but inhibits turnover of the lld-tripeptide. The mechanism by which this inhibition takes place is not fully understood. Recent studies have employed a range of lld-configured depsipeptide substrate analogues in crystallographic studies to probe events preceding beta-lactam closure in the IPNS reaction cycle. Herein, we report the first crystal structure of IPNS in complex with an lll-configured depsipeptide analogue, delta-l-alpha-aminoadipoyl-l-cysteine (1-(R)-carboxy-2-thiomethyl)ethyl ester (lll-ACOmC). This report describes the crystal structure of the IPNS:Fe(ii):lll-ACOmC complex to 2.0 A resolution, and discusses attempts to oxygenate this complex at high pressure in order to probe the mechanism by which lll-configured substrates inhibit IPNS catalysis. The crystal structure of an LLL-configured depsipeptide substrate analogue bound to isopenicillin N synthase.,Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ Org Biomol Chem. 2010 Jan 7;8(1):122-7. doi: 10.1039/b910170e. Epub 2009 Oct 29. PMID:20024142 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isopenicillin N synthase

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