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| | <StructureSection load='1ro5' size='340' side='right'caption='[[1ro5]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1ro5' size='340' side='right'caption='[[1ro5]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ro5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RO5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ro5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RO5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k4j|1k4j]], [[1kzf|1kzf]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LASI, PA1432 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=1ro5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro5 OCA], [https://pdbe.org/1ro5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ro5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ro5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ro5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro5 OCA], [http://pdbe.org/1ro5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ro5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ro5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LASI_PSEAE LASI_PSEAE]] Required for the synthesis of PAI consisting of 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3-oxododecanoyl)homoserine lactone, an autoinducer molecule which binds to LasR and thus acts in elastase biosynthesis regulation. | + | [https://www.uniprot.org/uniprot/LASI_PSEAE LASI_PSEAE] Required for the synthesis of PAI consisting of 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3-oxododecanoyl)homoserine lactone, an autoinducer molecule which binds to LasR and thus acts in elastase biosynthesis regulation. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Churchill, M E]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Gould, T A]] | + | [[Category: Churchill ME]] |
| - | [[Category: Schweizer, H P]] | + | [[Category: Gould TA]] |
| - | [[Category: Alpha-beta-alpha sandwich]] | + | [[Category: Schweizer HP]] |
| - | [[Category: Phosphopantetheine fold]]
| + | |
| - | [[Category: Signaling protein]]
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| Structural highlights
Function
LASI_PSEAE Required for the synthesis of PAI consisting of 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3-oxododecanoyl)homoserine lactone, an autoinducer molecule which binds to LasR and thus acts in elastase biosynthesis regulation.
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
The LasI/LasR quorum-sensing system plays a pivotal role in virulence gene regulation of the opportunistic human pathogen, Pseudomonas aeruginosa. Here we report the crystal structure of the acyl-homoserine lactone (AHL) synthase LasI that produces 3-oxo-C12-AHL from the substrates 3-oxo-C12-acyl-carrier protein (acyl-ACP) and S-adenosyl-L-methionine. The LasI six-stranded beta sheet platform, buttressed by three alpha helices, forms a V-shaped substrate-binding cleft that leads to a tunnel passing through the enzyme that can accommodate the acyl-chain of acyl-ACP. This tunnel places no apparent restriction on acyl-chain length, in contrast to a restrictive hydrophobic pocket seen in the AHL-synthase EsaI. Interactions of essential conserved N-terminal residues, Arg23, Phe27 and Trp33, suggest that the N-terminus forms an enclosed substrate-binding pocket for S-adenosyl-L-methionine. Analysis of AHL-synthase surface residues identified a binding site for acyl-ACP, a role that was supported by in vivo reporter assay analysis of the mutated residues, including Arg154 and Lys150. This structure and the novel explanation of AHL-synthase acyl-chain-length selectivity promise to guide the design of Pseudomonas aeruginosa-specific quorum-sensing inhibitors as antibacterial agents.
Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI.,Gould TA, Schweizer HP, Churchill ME Mol Microbiol. 2004 Aug;53(4):1135-46. PMID:15306017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gould TA, Schweizer HP, Churchill ME. Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI. Mol Microbiol. 2004 Aug;53(4):1135-46. PMID:15306017 doi:10.1111/j.1365-2958.2004.04211.x
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