1kzf: Difference between revisions
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==Crystal Structure of the Acyl-homoserine Lactone Synthase, EsaI== | |||
<StructureSection load='1kzf' size='340' side='right'caption='[[1kzf]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1kzf]] 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=1KZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KZF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=1kzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzf OCA], [https://pdbe.org/1kzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kzf RCSB], [https://www.ebi.ac.uk/pdbsum/1kzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzf ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
== | Check<jmol> | ||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kz/1kzf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1kzf ConSurf]. | |||
<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. | 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 1kzf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pantoea stewartii subsp. stewartii]] | [[Category: Pantoea stewartii subsp. stewartii]] | ||
[[Category: | [[Category: Beck von Bodman S]] | ||
[[Category: Churchill MEA]] | |||
[[Category: Churchill | [[Category: Minogue TD]] | ||
[[Category: Minogue | [[Category: Val DL]] | ||
[[Category: Val | [[Category: Watson WT]] | ||
[[Category: Watson | |||
