This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1djm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:24, 22 May 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1djm.jpg|left|200px]]
 
-
{{Structure
+
==SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI==
-
|PDB= 1djm |SIZE=350|CAPTION= <scene name='initialview01'>1djm</scene>
+
<StructureSection load='1djm' size='340' side='right'caption='[[1djm]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<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>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1djm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1djm OCA], [http://www.ebi.ac.uk/pdbsum/1djm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1djm RCSB]</span>
+
[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>
-
==Overview==
+
==See Also==
-
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.
+
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1DJM is a [[Single protein]] structure of sequence 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=1DJM OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/10731410 10731410]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Cho, H S.]]
+
[[Category: Cho HS]]
-
[[Category: Kustu, S.]]
+
[[Category: Kustu S]]
-
[[Category: Lee, S Y.]]
+
[[Category: Lee SY]]
-
[[Category: Pan, X.]]
+
[[Category: Pan X]]
-
[[Category: Parkinson, J S.]]
+
[[Category: Parkinson JS]]
-
[[Category: Pelton, J G.]]
+
[[Category: Pelton JG]]
-
[[Category: Wemmer, D E.]]
+
[[Category: Wemmer DE]]
-
[[Category: Yan, D.]]
+
[[Category: Yan D]]
-
[[Category: befx]]
+
-
[[Category: chemotaxis]]
+
-
[[Category: chey]]
+
-
[[Category: response regulator]]
+
-
[[Category: two-component]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:49 2008''
+

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