3HQT

PLP-Dependent Acyl-CoA Transferase CqsA

Summary for 3HQT

• Entry DOI: 10.2210/pdb3hqt/pdb
• Related: 3HQS
• Descriptor: CAI-1 autoinducer synthase, PYRIDOXAL-5'-PHOSPHATE (2 entities in total)
• Functional Keywords: quorum sensing, vibrio cholerae, cqsa, cai-1, autoinducer, plp, virulence, acyltransferase, aminotransferase, pyridoxal phosphate, transferase
• Biological source: Vibrio cholerae
• Total number of polymer chains: 2
• Total formula weight: 92119.97

Authors

Kelly, R.C.,Jeffrey, P.D.,Hughson, F.M. (deposition date: 2009-06-08, release date: 2009-10-20, Last modification date: 2023-09-06)

Primary citation

Kelly, R.C.,Bolitho, M.E.,Higgins, D.A.,Lu, W.,Ng, W.L.,Jeffrey, P.D.,Rabinowitz, J.D.,Semmelhack, M.F.,Hughson, F.M.,Bassler, B.L.
The Vibrio cholerae quorum-sensing autoinducer CAI-1: analysis of the biosynthetic enzyme CqsA.
Nat.Chem.Biol., 5:891-895, 2009

PubMed Abstract: Vibrio cholerae, the bacterium that causes the disease cholera, controls virulence factor production and biofilm development in response to two extracellular quorum-sensing molecules, called autoinducers. The strongest autoinducer, called CAI-1 (for cholera autoinducer-1), was previously identified as (S)-3-hydroxytridecan-4-one. Biosynthesis of CAI-1 requires the enzyme CqsA. Here, we determine the CqsA reaction mechanism, identify the CqsA substrates as (S)-2-aminobutyrate and decanoyl coenzyme A, and demonstrate that the product of the reaction is 3-aminotridecan-4-one, dubbed amino-CAI-1. CqsA produces amino-CAI-1 by a pyridoxal phosphate-dependent acyl-CoA transferase reaction. Amino-CAI-1 is converted to CAI-1 in a subsequent step via a CqsA-independent mechanism. Consistent with this, we find cells release > or =100 times more CAI-1 than amino-CAI-1. Nonetheless, V. cholerae responds to amino-CAI-1 as well as CAI-1, whereas other CAI-1 variants do not elicit a quorum-sensing response. Thus, both CAI-1 and amino-CAI-1 have potential as lead molecules in the development of an anticholera treatment.

PubMed: 19838203
DOI: 10.1038/nchembio.237

Experimental method

X-RAY DIFFRACTION (2.7 Å)