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| | ==Structure of Plp_Thr aldimine form of Vibrio cholerae CqsA== | | ==Structure of Plp_Thr aldimine form of Vibrio cholerae CqsA== |
| - | <StructureSection load='2wk9' size='340' side='right' caption='[[2wk9]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='2wk9' size='340' side='right'caption='[[2wk9]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wk9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WK9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wk9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WK9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wk7|2wk7]], [[2wka|2wka]], [[2wk8|2wk8]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wk9 OCA], [http://pdbe.org/2wk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wk9 RCSB], [http://www.ebi.ac.uk/pdbsum/2wk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wk9 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wk9 OCA], [https://pdbe.org/2wk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wk9 RCSB], [https://www.ebi.ac.uk/pdbsum/2wk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wk9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CQSA_VIBCH 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. | + | [https://www.uniprot.org/uniprot/CQSA_VIBCH 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibch]] | + | [[Category: Large Structures]] |
| - | [[Category: Botting, C H]] | + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] |
| - | [[Category: Jahan, N]] | + | [[Category: Botting CH]] |
| - | [[Category: Potter, J A]] | + | [[Category: Jahan N]] |
| - | [[Category: Sheikh, M A]] | + | [[Category: Potter JA]] |
| - | [[Category: Shirran, S L]] | + | [[Category: Sheikh MA]] |
| - | [[Category: Taylor, G L]] | + | [[Category: Shirran SL]] |
| - | [[Category: Westwood, N J]] | + | [[Category: Taylor GL]] |
| - | [[Category: Acyltransferase]]
| + | [[Category: Westwood NJ]] |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Autoinducer]]
| + | |
| - | [[Category: Cai-1]]
| + | |
| - | [[Category: Cqsa]]
| + | |
| - | [[Category: Oxoamine-synthase]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Quorum-sensing]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jahan N, Potter JA, Sheikh MA, Botting CH, Shirran SL, Westwood NJ, Taylor GL. Insights into the biosynthesis of the Vibrio cholerae major autoinducer CAI-1 from the crystal structure of the PLP-dependent enzyme CqsA. J Mol Biol. 2009 Sep 25;392(3):763-73. Epub 2009 Jul 22. PMID:19631226 doi:10.1016/j.jmb.2009.07.042
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