1ro5
From Proteopedia
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- | [[Image:1ro5.gif|left|200px]] | + | [[Image:1ro5.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure of the AHL Synthase LasI''' | + | {{Structure |
+ | |PDB= 1ro5 |SIZE=350|CAPTION= <scene name='initialview01'>1ro5</scene>, resolution 2.30Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= LASI, PA1432 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of the AHL Synthase LasI''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1RO5 is a [ | + | 1RO5 is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==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:[http:// | + | Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI., Gould TA, Schweizer HP, Churchill ME, Mol Microbiol. 2004 Aug;53(4):1135-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15306017 15306017] |
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phosphopantetheine fold]] | [[Category: phosphopantetheine fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:54:07 2008'' |
Revision as of 11:54, 20 March 2008
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, resolution 2.30Å | |||||||
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Ligands: | and | ||||||
Gene: | LASI, PA1432 (Pseudomonas aeruginosa) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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