6WNS
The structure of a CoA-dependent acyl-homoserine lactone synthase, MesI
6WNS の概要
| エントリーDOI | 10.2210/pdb6wns/pdb |
| 分子名称 | Acyl-homoserine-lactone synthase (2 entities in total) |
| 機能のキーワード | acyl-homoserine lactone, coenzyme a, mesi, transferase |
| 由来する生物種 | Mesorhizobium sp. ORS 3359 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 23120.88 |
| 構造登録者 | |
| 主引用文献 | Dong, S.H.,Nhu-Lam, M.,Nagarajan, R.,Nair, S.K. Structure-Guided Biochemical Analysis of Quorum Signal Synthase Specificities. Acs Chem.Biol., 15:1497-1504, 2020 Cited by PubMed Abstract: Many bacteria use membrane-diffusible small molecule quorum signals to coordinate gene transcription in response to changes in cell density, known as quorum sensing (QS). Among these, acyl-homoserine lactones (AHL) are widely distributed in and are involved in controlling the expression of virulence genes and biofilm formation in pathogens, such as . AHL molecules are specifically biosynthesized by the cognate LuxI type AHL synthases using -adenosylmethionine (SAM) and either acyl carrier protein (ACP)- or CoA-coupled fatty acids through a two-step reaction. Here, we characterize a CoA-dependent LuxI synthase from that utilizes an aryl-CoA substrate that is environmentally derived, specifically -coumaric acid. We leverage structures of this aryl-CoA-dependent synthase, along with our prior studies of an acyl-CoA-dependent synthase, to identify residues that confer substrate chain specificity in these enzymes. We test our predictions by carrying out biochemical, kinetic, and structural characterization of representative AHL signal synthases. Our studies provide an understanding of various AHL synthases that may be deployed in synthetic biological applications and inform on the design of specific small molecule therapeutics that can restrict virulence by targeting quorum signaling. PubMed: 32356962DOI: 10.1021/acschembio.0c00142 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.93 Å) |
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