2bu9 | pdb_00002bu9

Isopenicillin N synthase complexed with L-aminoadipoyl-L-cysteinyl-L- hexafluorovaline

spinqualitylabelsall models 2bu9, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bu9 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: FE, HFV, SO4 Related: 1bk0, 1blz, 1hb1, 1hb2, 1hb3, 1hb4, 1ips, 1obn, 1oc1, 1odm, 1odn, 1qiq, 1qje, 1qjf, 1uzw, 1w03, 1w04, 1w05, 1w06, 1w3v, 1w3x, 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-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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isopenicillin N synthase

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