2Y60

Isopenicillin N synthase with AC-D-methionine

2Y60 の概要

• エントリーDOI: 10.2210/pdb2y60/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 2BU9 2IVI 2IVJ 2JB4 2VAU 2VBB 2VBD 2VBP 2VCM 2VE1 2WO7
• 分子名称: ISOPENICILLIN N SYNTHASE, N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-methionine, FE (III) ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, oxygenase, penicillin biosynthesis
• 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: 38299.40

構造登録者

Rutledge, P.J.,Clifton, I.J.,Ge, W. (登録日: 2011-01-19, 公開日: 2012-02-08, 最終更新日: 2024-05-08)

主引用文献

Clifton, I.J.,Ge, W.,Adlington, R.M.,Baldwin, J.E.,Rutledge, P.J.
The Crystal Structure of Isopenicillin N Synthase with Delta((L)-Alpha-Aminoadipoyl)-(L)-Cysteinyl-(D)-Methionine Reveals Thioether Coordination to Iron.
Arch.Biochem.Biophys., 516:103-, 2011

PubMed Abstract: Isopenicillin N synthase (IPNS) catalyses cyclization of δ-(l-α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) to isopenicillin N (IPN), the central step in penicillin biosynthesis. Previous studies have shown that IPNS turns over a wide range of substrate analogues in which the valine residue of its natural substrate is replaced with other amino acids. IPNS accepts and oxidizes numerous substrates that bear hydrocarbon sidechains in this position, however the enzyme is less tolerant of analogues presenting polar functionality in place of the valinyl isopropyl group. We report a new ACV analogue δ-(l-α-aminoadipoyl)-l-cysteinyl-d-methionine (ACM), which incorporates a thioether in place of the valinyl sidechain. ACM has been synthesized using solution phase methods and crystallized with IPNS. A crystal structure has been elucidated for the IPNS:Fe(II):ACM complex at 1.40Å resolution. This structure reveals that ACM binds in the IPNS active site such that the sulfur atom of the methionine thioether binds to iron in the oxygen binding site at a distance of 2.57Å. The sulfur of the cysteinyl thiolate sits 2.36Å from the metal.

PubMed: 22001738
DOI: 10.1016/J.ABB.2011.09.014

実験手法

X-RAY DIFFRACTION (1.4 Å)