3HQT
PLP-Dependent Acyl-CoA Transferase CqsA
3HQT の概要
エントリーDOI | 10.2210/pdb3hqt/pdb |
関連するPDBエントリー | 3HQS |
分子名称 | CAI-1 autoinducer synthase, PYRIDOXAL-5'-PHOSPHATE (2 entities in total) |
機能のキーワード | quorum sensing, vibrio cholerae, cqsa, cai-1, autoinducer, plp, virulence, acyltransferase, aminotransferase, pyridoxal phosphate, transferase |
由来する生物種 | Vibrio cholerae |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 92119.97 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 19838203DOI: 10.1038/nchembio.237 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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