3zoi | pdb_00003zoi

ISOPENICILLIN N SYNTHASE WITH AC-O-METHYL-D-THREONINE

spinqualitylabelsall models 3zoi, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zoi is a 1 chain structure with sequence from A. nidulans. This structure supersedes the now removed PDB entry 2y86. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, GOL, M2W, SO4 Activity: Isopenicillin-N synthase, with EC number 1.21.3.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Isopenicillin N synthase (IPNS) is a non-heme iron oxidase central to the biosynthesis of beta-lactam antibiotics. IPNS converts the tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N while reducing molecular oxygen to water. The substrate analogue delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine (ACmT) is not turned over by IPNS. Epimeric delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine (ACmaT) is converted to a bioactive penam product. ACmT and ACmaT differ from each other only in the stereochemistry at the beta-carbon atom of their third residue. These substrates both contain a methyl ether in place of the isopropyl group of ACV. We report an X-ray crystal structure for the anaerobic IPNS:Fe(II):ACmT complex. This structure reveals an additional water molecule bound to the active site metal, held by hydrogen-bonding to the ether oxygen atom of the substrate analogue. The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site.,Clifton IJ, Ge W, Adlington RM, Baldwin JE, Rutledge PJ FEBS Lett. 2013 Aug 19;587(16):2705-9. doi: 10.1016/j.febslet.2013.07.016. Epub, 2013 Jul 13. PMID:23860486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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