This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ro5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:09, 8 March 2018

Crystal Structure of the AHL Synthase LasI

Structural highlights

1ro5 is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1k4j, 1kzf
Gene:	LASI, PA1432 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ro5"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the AHL Synthase LasI==
 <StructureSection load='1ro5' size='340' side='right' caption='[[1ro5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k4j|1k4j]], [[1kzf|1kzf]]</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'>[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://pdbe.org/1ro5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ro5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ro5 PDBsum]</span></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=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>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ro5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ro5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1ro5

From Proteopedia

Revision as of 07:09, 8 March 2018

Crystal Structure of the AHL Synthase LasI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox