6ULZ

Adenylation domain of the initiation module of LgrA mutant P483M

6ULZ の概要

• エントリーDOI: 10.2210/pdb6ulz/pdb
• 分子名称: Linear gramicidin synthase subunit A, FORMIC ACID, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (5 entities in total)
• 機能のキーワード: nrps, nonribosomal peptide synthetase, non-ribosomal peptide synthetase, adenylation, adenylation domain, natural product, adenylate, biosynthetic protein
• 由来する生物種: Brevibacillus parabrevis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 78504.89

構造登録者

Chiche-Lapierre, C.,Alonzo, D.A.,Schmeing, T.M. (登録日: 2019-10-08, 公開日: 2020-02-19, 最終更新日: 2023-10-11)

主引用文献

Alonzo, D.A.,Chiche-Lapierre, C.,Tarry, M.J.,Wang, J.,Schmeing, T.M.
Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis.
Nat.Chem.Biol., 16:493-496, 2020

PubMed Abstract: Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from α-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for α-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoA' domain, structurally important for the depsipeptide module's synthetic cycle.

PubMed: 32066969
DOI: 10.1038/s41589-020-0481-5

実験手法

X-RAY DIFFRACTION (3.1 Å)