| Structural highlights
2bu9 is a 1 chain structure with sequence from Emericella 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 |
| 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) 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Howard-Jones AR, Rutledge PJ, Clifton IJ, Adlington RM, Baldwin JE. Unique binding of a non-natural L,L,L-substrate by isopenicillin N synthase. Biochem Biophys Res Commun. 2005 Oct 21;336(2):702-8. PMID:16143309 doi:10.1016/j.bbrc.2005.08.155
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