2wka | pdb_00002wka

Structure of Plp_Thr_decanoyl-CoA aldimine form of Vibrio cholerae CqsA

spinqualitylabelsall models 2wka, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wka is a 2 chain structure with sequence from Vibch. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, P89, SO4 Related: 2wk7, 2wk8, 2wk9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CQSA_VIBCH] Required for the synthesis of the quorum-sensing autoinducer CAI-1 ((S)-3-hydroxytridecan-4-one) which probably functions as an intragenus signal. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed CqsA is an enzyme involved in the biosynthesis of cholerae autoinducer-1 (CAI-1), the major Vibrio cholerae autoinducer engaged in quorum sensing. The amino acid sequence of CqsA suggests that it belongs to the family of alpha-oxoamine synthases that catalyse the condensation of an amino acid to an acyl-CoA substrate. Here we present the apo- and PLP-bound crystal structures of CqsA and confirm that it shares structural homology with the dimeric alpha-oxoamine synthases, including a conserved PLP-binding site. The chemical structure of CAI-1 suggests that decanoyl-CoA may be one substrate of CqsA and that another substrate may be l-threonine or l-2-aminobutyric acid. A crystal structure of CqsA at 1.9-A resolution obtained in the presence of PLP and l-threonine reveals an external aldimine that has lost the l-threonine side chain. Similarly, a 1.9-A-resolution crystal structure of CqsA in the presence of PLP, l-threonine, and decanoyl-CoA shows a trapped external aldimine intermediate, suggesting that the condensation and decarboxylation steps have occurred, again with loss of the l-threonine side chain. It is suggested that this side-chain loss, an observation supported by mass spectrometry, is due to a retro-aldol reaction. Although no structural data have been obtained on CqsA using l-2-aminobutyric acid and decanoyl-CoA as substrates, mass spectrometry confirms the expected product of the enzyme reaction. It is proposed that a region of structure that is disordered in the apo structure is involved in the release of product. While not confirming if CqsA alone is able to synthesize CAI-1, these results suggest possible synthetic routes. Insights into the biosynthesis of the Vibrio cholerae major autoinducer CAI-1 from the crystal structure of the PLP-dependent enzyme CqsA.,Jahan N, Potter JA, Sheikh MA, Botting CH, Shirran SL, Westwood NJ, Taylor GL J Mol Biol. 2009 Sep 25;392(3):763-73. Epub 2009 Jul 22. PMID:19631226 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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