5W8A

The structure of a COA-dependent acyl-homoserine lactone synthase, BjaI, with SAM and isopentyl-CoA

5W8A の概要

• エントリーDOI: 10.2210/pdb5w8a/pdb
• 分子名称: Autoinducer synthase, S-ADENOSYLMETHIONINE, isopentyl-Coenzyme A, ... (4 entities in total)
• 機能のキーワード: acyl-homoserine lactone, coenzyme a, bjai, biosynthetic protein
• 由来する生物種: Bradyrhizobium japonicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26405.84

構造登録者

Dong, S.-H.,Nair, S.K. (登録日: 2017-06-21, 公開日: 2017-08-23, 最終更新日: 2024-03-13)

主引用文献

Dong, S.H.,Frane, N.D.,Christensen, Q.H.,Greenberg, E.P.,Nagarajan, R.,Nair, S.K.
Molecular basis for the substrate specificity of quorum signal synthases.
Proc. Natl. Acad. Sci. U.S.A., 114:9092-9097, 2017

PubMed Abstract: In several , LuxI-type enzymes catalyze the biosynthesis of acyl-homoserine lactones (AHL) signals using -adenosyl-l-methionine and either cellular acyl carrier protein (ACP)-coupled fatty acids or CoA-aryl/acyl moieties as progenitors. Little is known about the molecular mechanism of signal biosynthesis, the basis for substrate specificity, or the rationale for donor specificity for any LuxI member. Here, we present several cocrystal structures of BjaI, a CoA-dependent LuxI homolog that represent views of enzyme complexes that exist along the reaction coordinate of signal synthesis. Complementary biophysical, structure-function, and kinetic analysis define the features that facilitate the unusual acyl conjugation with -adenosylmethionine (SAM). We also identify the determinant that establishes specificity for the acyl donor and identify residues that are critical for acyl/aryl specificity. These results highlight how a prevalent scaffold has evolved to catalyze quorum signal synthesis and provide a framework for the design of small-molecule antagonists of quorum signaling.

PubMed: 28784791
DOI: 10.1073/pnas.1705400114

実験手法

X-RAY DIFFRACTION (2 Å)