1eay

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{{Seed}}
 
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[[Image:1eay.png|left|200px]]
 
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==CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI==
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The line below this paragraph, containing "STRUCTURE_1eay", creates the "Structure Box" on the page.
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<StructureSection load='1eay' size='340' side='right'caption='[[1eay]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1eay]] is a 4 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=1EAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eay OCA], [https://pdbe.org/1eay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eay RCSB], [https://www.ebi.ac.uk/pdbsum/1eay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eay ProSAT]</span></td></tr>
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{{STRUCTURE_1eay| PDB=1eay | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/1eay_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eay ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure at 2.0-A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain (P2) of the kinase CheA is presented. The binding interface involves the fourth and fifth helices and fifth beta-strand of CheY and both helices of P2. Surprisingly, the two heterodimers in the asymmetric unit have two different binding modes involving the same interface, suggesting some flexibility in the binding regions. Significant conformational changes have occurred in CheY compared with previously determined unbound structures. The active site of CheY is exposed by the binding of the kinase domain, possibly to enhance phosphotransfer from CheA to CheY. The conformational changes upon complex formation as well as the observation that there are two different binding modes suggest that the plasticity of CheY is an essential feature of response regulator function.
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===CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI===
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Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.,McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. PMID:9636149<ref>PMID:9636149</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_9636149}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1eay" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9636149 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9636149}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1EAY 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=1EAY OCA].
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==Reference==
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Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway., McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW, Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9636149 9636149]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Dahlquist, F W.]]
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[[Category: Dahlquist FW]]
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[[Category: Hausrath, A C.]]
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[[Category: Hausrath AC]]
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[[Category: Mcevoy, M M.]]
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[[Category: Mcevoy MM]]
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[[Category: Randolph, G B.]]
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[[Category: Randolph GB]]
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[[Category: Remington, S J.]]
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[[Category: Remington SJ]]
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[[Category: Chemotaxis]]
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[[Category: Kinase]]
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[[Category: Response regulator]]
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[[Category: Signal transduction complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:25:51 2008''
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Current revision

CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI

PDB ID 1eay

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