2JGP

Structure of the TycC5-6 PCP-C bidomain of the tyrocidine synthetase TycC

2JGP の概要

• エントリーDOI: 10.2210/pdb2jgp/pdb
• 関連するPDBエントリー: 1DNY
• 分子名称: TYROCIDINE SYNTHETASE 3, SULFATE ION, 1,4-DIETHYLENE DIOXIDE, ... (5 entities in total)
• 機能のキーワード: multifunctional enzyme, antibiotic biosynthesis, condensation domain, peptide bond formation, ligase, tyrocidine, antibiotics, phosphopantetheine, nonribosomal peptide synthetase, peptidyl carrier domain
• 由来する生物種: BREVIBACILLUS BREVIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59295.73

構造登録者

Samel, S.A.,Schoenafinger, G.,Knappe, T.A.,Marahiel, M.A.,Essen, L.-O. (登録日: 2007-02-13, 公開日: 2007-10-30, 最終更新日: 2024-05-08)

主引用文献

Samel, S.A.,Schoenafinger, G.,Knappe, T.A.,Marahiel, M.A.,Essen, L.-O.
Structural and Functional Insights Into a Peptide Bond-Forming Bidomain from a Nonribosomal Peptide Synthetase.
Structure, 15:781-, 2007

PubMed Abstract: The crystal structure of the bidomain PCP-C from modules 5 and 6 of the nonribosomal tyrocidine synthetase TycC was determined at 1.8 A resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of which is associated with the preceding peptidyl carrier protein (PCP) domain at its donor side. The relative arrangement of the PCP and the peptide bond-forming condensation (C) domain places the active sites approximately 50 A apart. Accordingly, this PCP-C structure represents a conformational state prior to peptide transfer from the donor-PCP to the acceptor-PCP domain, implying the existence of additional states of PCP-C domain interaction during catalysis. Additionally, PCP-C exerts a mode of cyclization activity that mimics peptide bond formation catalyzed by C domains. Based on mutational data and pK value analysis of active site residues, it is suggested that nonribosomal peptide bond formation depends on electrostatic interactions rather than on general acid/base catalysis.

PubMed: 17637339
DOI: 10.1016/J.STR.2007.05.008

実験手法

X-RAY DIFFRACTION (1.85 Å)