6wn0 | pdb_00006wn0

The structure of a CoA-dependent acyl-homoserine lactone synthase, RpaI, with the adduct of SAH and p-coumaroyl CoA

spinqualitylabelsall models 6wn0, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6wn0 is a 2 chain structure with sequence from Rhodopseudomonas palustris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: COA, U4Y Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RPAI_RHOPA Catalyzes the synthesis of 4-coumaroyl-homoserine lactone, a quorum-sensing (QS) autoinducer molecule which binds to RpaR transcriptional regulator to regulate expression of QS-dependent genes. Publication Abstract from PubMed 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 wide distributed in Proteobacteria, and are involved in controlling the expression of virulence genes and biofilm formation in pathogens, such as Pseudomonas aeruginosa. AHL molecules are specifically biosynthesized by the cognate LuxI type AHL synthases using S-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 Rhodopseudomonas palustris that utilizes an aryl-CoA substrate that is environmentally derived, specifically p-coumaric acid. We leverage structures of this aryl-CoA-dependent synthase, along with our prior studies of an acyl-CoA 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 signalling. Structure-Guided Biochemical Analysis of Quorum Signal Synthase Specificities.,Dong SH, Nhu-Lam M, Nagarajan R, Nair SK ACS Chem Biol. 2020 May 1. doi: 10.1021/acschembio.0c00142. PMID:32356962 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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