1k4j
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='1k4j' size='340' side='right'caption='[[1k4j]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1k4j' size='340' side='right'caption='[[1k4j]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1k4j]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1k4j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pantoea_stewartii_subsp._stewartii Pantoea stewartii subsp. stewartii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K4J FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=REO:PERRHENATE'>REO</scene></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=1k4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4j OCA], [https://pdbe.org/1k4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k4j RCSB], [https://www.ebi.ac.uk/pdbsum/1k4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4j ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/ESAI_PANSE ESAI_PANSE] Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-homoserine lactone), an autoinducer molecule which binds to EsaR. OHHL is necessary for biosynthesis of EPS virulence factor (extracellular heteropolysaccharide) which plays a role in the development of Stewart's wilt on sweet corn. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 21: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k4j ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k4j ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Synthesis and detection of acyl-homoserine lactones (AHLs) enables many gram-negative bacteria to engage in quorum sensing, an intercellular signaling mechanism that activates differentiation to virulent and biofilm lifestyles. The AHL synthases catalyze acylation of S-adenosyl-L-methionine by acyl-acyl carrier protein and lactonization of the methionine moiety to give AHLs. The crystal structure of the AHL synthase, EsaI, determined at 1.8 A resolution, reveals a remarkable structural similarity to the N-acetyltransferases and defines a common phosphopantetheine binding fold as the catalytic core. Critical residues responsible for catalysis and acyl chain specificity have been identified from a modeled substrate complex and verified through functional analysis in vivo. A mechanism for the N-acylation of S-adenosyl-L-methionine by 3-oxo-hexanoyl-acyl carrier protein is proposed. | ||
- | |||
- | Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing.,Watson WT, Minogue TD, Val DL, von Bodman SB, Churchill ME Mol Cell. 2002 Mar;9(3):685-94. PMID:11931774<ref>PMID:11931774</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1k4j" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Pantoea stewartii subsp. stewartii]] |
- | + | [[Category: Beck von Bodman S]] | |
- | [[Category: | + | [[Category: Churchill MEA]] |
- | [[Category: | + | [[Category: Minogue TD]] |
- | [[Category: | + | [[Category: Val DL]] |
- | [[Category: | + | [[Category: Watson WT]] |
- | [[Category: | + | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate
|