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1chn

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Revision as of 12:02, 11 September 2015

MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE

Structural highlights

1chn is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The three-dimensional crystal structure of the bacterial chemotaxis protein CheY with the essential Mg2+ cation bound to the active site reveals large conformational changes caused by the metal binding. Displacements of up to 10 A are observed in several residues at the N terminus of alpha-helix 4 and in the preceding loop. One turn of this helix unwinds, and an Asn residue that was located inside the helix becomes the new N-cap. This supports the important role that N or C-cap residues play in alpha-helix stability. In addition the preceding beta-strand becomes elongated and a new beta-turn appears. The final effect is a significant modification of the surface relief of the protein in a region previously indicated, by genetic analysis, to be essential for CheY function. It is suggested that binding of a divalent cation to CheY could play a significant part in CheY activation and consequently in signal transduction in prokaryotes.

Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface.,Bellsolell L, Prieto J, Serrano L, Coll M J Mol Biol. 1994 May 13;238(4):489-95. PMID:8176739^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM. The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol Cell. 2010 Apr 9;38(1):128-39. doi: 10.1016/j.molcel.2010.03.001. Epub 2010, Mar 25. PMID:20346719 doi:10.1016/j.molcel.2010.03.001
↑ Bellsolell L, Prieto J, Serrano L, Coll M. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J Mol Biol. 1994 May 13;238(4):489-95. PMID:8176739 doi:http://dx.doi.org/10.1006/jmbi.1994.1308

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1chn"

Categories: Bacillus coli migula 1895 | Bellsolell, L | Coll, M | Signal transduction protein

@@ Line 2: / Line 2: @@
 <StructureSection load='1chn' size='340' side='right' caption='[[1chn]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1chn]] is a 1 chain structure with 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=1CHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CHN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1chn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CHN FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1chn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1chn RCSB], [http://www.ebi.ac.uk/pdbsum/1chn PDBsum]</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=1chn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chn OCA], [http://pdbe.org/1chn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1chn RCSB], [http://www.ebi.ac.uk/pdbsum/1chn PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1chn" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Bellsolell, L]]
 [[Category: Coll, M]]
 [[Category: Signal transduction protein]]

1chn

From Proteopedia

Revision as of 12:02, 11 September 2015

MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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