3jyb: Difference between revisions
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== | ==Crystal Structure of the RetS periplasmic domain== | ||
[[3jyb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <StructureSection load='3jyb' size='340' side='right'caption='[[3jyb]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3jyb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseab Pseab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JYB FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA14_64230, PA4856, retS, rets (AMINO ACIDS 41 - 185) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=3jyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jyb OCA], [http://pdbe.org/3jyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jyb RCSB], [http://www.ebi.ac.uk/pdbsum/3jyb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jyb ProSAT]</span></td></tr> | |||
</table> | |||
== 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/jy/3jyb_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=3jyb ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The opportunistic pathogen Pseudomonas aeruginosa may cause both acute and chronic-persistent infections in predisposed individuals. Acute infections require the presence of a functional type III secretion system (T3SS), whereas chronic P. aeruginosa infections are characterized by the formation of drug-resistant biofilms. The T3SS and biofilm formation are reciprocally regulated by the signaling kinases LadS, RetS, and GacS. RetS downregulates biofilm formation and upregulates expression of the T3SS through a unique mechanism. RetS forms a heterodimeric complex with GacS and thus prevents GacS autophosphorylation and downstream signaling. The signals that regulate RetS are not known but RetS possesses a distinctive periplasmic sensor domain that is believed to serve as receptor for the regulatory ligand. We have determined the crystal structure of the RetS sensory domain at 2.0 A resolution. The structure closely resembles those of carbohydrate binding modules of other proteins, suggesting that the elusive ligands are likely carbohydrate moieties. In addition to the conserved beta-sandwich structure, the sensory domain features two alpha helices which create a unique surface topology. Protein-protein crosslinking and fluorescence energy transfer experiments also revealed that the sensory domain dimerizes with a dissociation constant of K(d) = 580 +/- 50 nM, a result with interesting implications for our understanding of the underlying signaling mechanism. Proteins 2010. (c) 2010 Wiley-Liss, Inc. | |||
Crystal structure and oligomeric state of the RetS signaling kinase sensory domain.,Jing X, Jaw J, Robinson HH, Schubot FD Proteins. 2009 Dec 21. PMID:20112417<ref>PMID:20112417</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3jyb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Histidine kinase]] | [[Category: Histidine kinase]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Jing, X | [[Category: Pseab]] | ||
[[Category: Robinson, H | [[Category: Jing, X]] | ||
[[Category: Schubot, F D | [[Category: Robinson, H]] | ||
[[Category: Schubot, F D]] | |||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Carbohydrate binding domain]] | [[Category: Carbohydrate binding domain]] | ||
