2VSQ

Structure of surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module

2VSQ の概要

• エントリーDOI: 10.2210/pdb2vsq/pdb
• 関連するPDBエントリー: 1JMK
• 分子名称: SURFACTIN SYNTHETASE SUBUNIT 3, LEUCINE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ligase, peptidyl carrier protein, ligase phosphoprotein, termination module, phosphopantetheine, nonribosomal peptide synthesis, synthetase, adenylation, sporulation, antibiotic biosynthesis, enzymatic assembly line, surfactin a, condensation, thioesterase
• 由来する生物種: BACILLUS SUBTILIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 147667.78

構造登録者

Tanovic, A.,Samel, S.A.,Essen, L.-O.,Marahiel, M.A. (登録日: 2008-04-29, 公開日: 2008-07-08, 最終更新日: 2023-12-13)

主引用文献

Tanovic, A.,Samel, S.A.,Essen, L.O.,Marahiel, M.A.
Crystal structure of the termination module of a nonribosomal peptide synthetase.
Science, 321:659-663, 2008

PubMed Abstract: Nonribosomal peptide synthetases (NRPSs) are modular multidomain enzymes that act as an assembly line to catalyze the biosynthesis of complex natural products. The crystal structure of the 144-kilodalton Bacillus subtilis termination module SrfA-C was solved at 2.6 angstrom resolution. The adenylation and condensation domains of SrfA-C associate closely to form a catalytic platform, with their active sites on the same side of the platform. The peptidyl carrier protein domain is flexibly tethered to this platform and thus can move with its substrate-loaded 4'-phosphopantetheine arm between the active site of the adenylation domain and the donor side of the condensation domain. The SrfA-C crystal structure has implications for the rational redesign of NRPSs as a means of producing novel bioactive peptides.

PubMed: 18583577
DOI: 10.1126/science.1159850

実験手法

X-RAY DIFFRACTION (2.6 Å)