5W8A

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

Summary for 5W8A

• Entry DOI: 10.2210/pdb5w8a/pdb
• Descriptor: Autoinducer synthase, S-ADENOSYLMETHIONINE, isopentyl-Coenzyme A, ... (4 entities in total)
• Functional Keywords: acyl-homoserine lactone, coenzyme a, bjai, biosynthetic protein
• Biological source: Bradyrhizobium japonicum
• Total number of polymer chains: 1
• Total formula weight: 26405.84

Authors

Dong, S.-H.,Nair, S.K. (deposition date: 2017-06-21, release date: 2017-08-23, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)