2BU9

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

2BU9 の概要

• エントリーDOI: 10.2210/pdb2bu9/pdb
• 関連するPDBエントリー: 1BK0 1BLZ 1HB1 1HB2 1HB3 1HB4 1IPS 1OBN 1OC1 1ODM 1ODN 1QIQ 1QJE 1QJF 1UZW 1W03 1W04 1W05 1W06 1W3V 1W3X 2BJS
• 分子名称: ISOPENICILLIN N SYNTHETASE, FE (III) ION, DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-L-3,3,3,3',3',3'-HEXAFLUOROVALINE, ... (5 entities in total)
• 機能のキーワード: b-lactam antibiotic, oxygenase, penicillin biosynthesis, antibiotic biosynthesis, oxidoreductase
• 由来する生物種: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38187.12

構造登録者

Howard-Jones, A.R.,Rutledge, P.J.,Clifton, I.J.,Adlington, R.M.,Baldwin, J.E. (登録日: 2005-06-09, 公開日: 2005-09-15, 最終更新日: 2024-05-08)

主引用文献

Howard-Jones, A.R.,Rutledge, P.J.,Clifton, I.J.,Adlington, R.M.,Baldwin, J.E.
Unique Binding of a Non-Natural L,L,L-Substrate by Isopenicillin N Synthase
Biochem.Biophys.Res.Commun., 336:702-, 2005

PubMed Abstract: 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.

PubMed: 16143309
DOI: 10.1016/J.BBRC.2005.08.155

実験手法

X-RAY DIFFRACTION (1.3 Å)