1bdj: Difference between revisions

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-{{Seed}}
-[[Image:1bdj.png|left|200px]]
-<!--
+==COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY==
-The line below this paragraph, containing "STRUCTURE_1bdj", creates the "Structure Box" on the page.
+<StructureSection load='1bdj' size='340' side='right'caption='[[1bdj]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1bdj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BDJ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1bdj|  PDB=1bdj  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bdj OCA], [https://pdbe.org/1bdj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bdj RCSB], [https://www.ebi.ac.uk/pdbsum/1bdj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bdj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHEY_ECOLI CHEY_ECOLI] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.<ref>PMID:20346719</ref>
+== 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/bd/1bdj_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=1bdj ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 A resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.
-===COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY===
+Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY.,Kato M, Shimizu T, Mizuno T, Hakoshima T Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1257-63. PMID:10393292<ref>PMID:10393292</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1bdj" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10393292}}, adds the Publication Abstract to the page
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10393292 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10393292}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BDJ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDJ OCA].
-==Reference==
-Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY., Kato M, Shimizu T, Mizuno T, Hakoshima T, Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1257-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10393292 10393292]
 [[Category: Escherichia coli]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Hakoshima, T.]]
+[[Category: Hakoshima T]]
-[[Category: Kato, M.]]
+[[Category: Kato M]]
-[[Category: Mizuno, T.]]
+[[Category: Mizuno T]]
-[[Category: Shimizu, T.]]
+[[Category: Shimizu T]]
-[[Category: Arcb]]
-[[Category: Chey]]
-[[Category: Response regulator]]
-[[Category: Two-component system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:54:09 2008''