1djm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:24, 22 May 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1djm.png|left|200px]]
 
-
<!--
+
==SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI==
-
The line below this paragraph, containing "STRUCTURE_1djm", creates the "Structure Box" on the page.
+
<StructureSection load='1djm' size='340' side='right'caption='[[1djm]]' 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'>[[1djm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJM 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">Solution NMR</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=1djm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1djm OCA], [https://pdbe.org/1djm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1djm RCSB], [https://www.ebi.ac.uk/pdbsum/1djm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1djm ProSAT]</span></td></tr>
-
{{STRUCTURE_1djm| PDB=1djm | SCENE= }}
+
</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/dj/1djm_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=1djm ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The CheY protein is the response regulator in bacterial chemotaxis. Phosphorylation of a conserved aspartyl residue induces structural changes that convert the protein from an inactive to an active state. The short half-life of the aspartyl-phosphate has precluded detailed structural analysis of the active protein. Persistent activation of Escherichia coli CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the structure determined by NMR spectroscopy to a backbone r.m.s.d. of 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The coupled rearrangement may be a more general mechanism for activation of receiver domains.
-
===SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI===
+
NMR structure of activated CheY.,Cho HS, Lee SY, Yan D, Pan X, Parkinson JS, Kustu S, Wemmer DE, Pelton JG J Mol Biol. 2000 Mar 31;297(3):543-51. PMID:10731410<ref>PMID:10731410</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1djm" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_10731410}}, 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 10731410 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_10731410}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1DJM is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJM OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:10731410</ref><references group="xtra"/>
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Cho, H S.]]
+
[[Category: Large Structures]]
-
[[Category: Kustu, S.]]
+
[[Category: Cho HS]]
-
[[Category: Lee, S Y.]]
+
[[Category: Kustu S]]
-
[[Category: Pan, X.]]
+
[[Category: Lee SY]]
-
[[Category: Parkinson, J S.]]
+
[[Category: Pan X]]
-
[[Category: Pelton, J G.]]
+
[[Category: Parkinson JS]]
-
[[Category: Wemmer, D E.]]
+
[[Category: Pelton JG]]
-
[[Category: Yan, D.]]
+
[[Category: Wemmer DE]]
-
[[Category: Befx]]
+
[[Category: Yan D]]
-
[[Category: Chemotaxis]]
+
-
[[Category: Chey]]
+
-
[[Category: Response regulator]]
+
-
[[Category: Two-component]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 22:00:39 2009''
+

Current revision

SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI

PDB ID 1djm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1djm"
Personal tools