1ro5

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[[Image:1ro5.gif|left|200px]]
[[Image:1ro5.gif|left|200px]]
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{{Structure
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|PDB= 1ro5 |SIZE=350|CAPTION= <scene name='initialview01'>1ro5</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1ro5", creates the "Structure Box" on the page.
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|GENE= LASI, PA1432 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
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{{STRUCTURE_1ro5| PDB=1ro5 | SCENE= }}
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|RELATEDENTRY=[[1k4j|1k4j]], [[1kzf|1kzf]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ro5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro5 OCA], [http://www.ebi.ac.uk/pdbsum/1ro5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ro5 RCSB]</span>
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'''Crystal Structure of the AHL Synthase LasI'''
'''Crystal Structure of the AHL Synthase LasI'''
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[[Category: Gould, T A.]]
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[[Category: Schweizer, H P.]]
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[[Category: Alpha-beta-alpha sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:43:10 2008''
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Revision as of 04:43, 3 May 2008

Template:STRUCTURE 1ro5

Crystal Structure of the AHL Synthase LasI


Overview

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.

About this Structure

1RO5 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 07:43:10 2008

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