| Structural highlights
2ivj 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: | , ,
| | Related: | 1bk0, 1blz, 1hb1, 1hb2, 1hb3, 1hb4, 1ips, 1obn, 1oc1, 1odm, 1odn, 1qiq, 1qje, 1qjf, 1uzw, 1w03, 1w04, 1w05, 1w06, 1w3v, 1w3x, 2bjs, 2bu9, 2ivi |
| Activity: | Isopenicillin-N synthase, with EC number 1.21.3.1 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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), a non-heme iron oxidase central to penicillin and cephalosporin biosynthesis, catalyzes an energetically demanding chemical transformation to produce isopenicillin N from the tripeptide delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-valine (ACV). We describe the synthesis of two cyclopropyl-containing tripeptide analogues, delta-(l-alpha-aminoadipoyl)-l-cysteinyl-beta-methyl-d-cyclopropylglycine and delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-cyclopropylglycine, designed as probes for the mechanism of IPNS. We have solved the X-ray crystal structures of these substrates in complex with IPNS and propose a revised mechanism for the IPNS-mediated turnover of these compounds. Relative to the previously determined IPNS-Fe(II)-ACV structure, key differences exist in substrate orientation and water occupancy, which allow for an explanation of the differences in reactivity of these substrates.
Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight.,Howard-Jones AR, Elkins JM, Clifton IJ, Roach PL, Adlington RM, Baldwin JE, Rutledge PJ Biochemistry. 2007 Apr 24;46(16):4755-62. Epub 2007 Mar 31. PMID:17397141[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Howard-Jones AR, Elkins JM, Clifton IJ, Roach PL, Adlington RM, Baldwin JE, Rutledge PJ. Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight. Biochemistry. 2007 Apr 24;46(16):4755-62. Epub 2007 Mar 31. PMID:17397141 doi:10.1021/bi062314q
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