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2id7

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Revision as of 08:28, 18 October 2017

1.75 A Structure of T87I Phosphono-CheY

Structural highlights

2id7 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.
NonStd Res:
Related:	1c4w
Gene:	cheY ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

CheY is a response regulator in bacterial chemotaxis. Escherichia coli CheY mutants T87I and T87I/Y106W CheY are phosphorylatable on Asp57 but unable to generate clockwise rotation of the flagella. To understand this phenotype in terms of structure, stable analogs of the two CheY-P mutants were synthesized: T87I phosphono-CheY and T87I phosphono-CheY. Dissociation constants for peptides derived from flagellar motor protein FliM and phosphatase CheZ were determined for phosphono-CheY and the two mutants. The peptides bind phosphono-CheY almost as strongly as CheY-P; however, they do not bind T87I phosphono-CheY or T87I/Y106W phosphono-CheY, implying that the mutant proteins cannot bind FliM or CheZ tightly in vivo. The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY were solved to resolutions of 1.8 and 2.4A, respectively. The increased bulk of I87 forces the side-chain of Y106 or W106, into a more solvent-accessible conformation, which occludes the peptide-binding site.

The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides.,McAdams K, Casper ES, Matthew Haas R, Santarsiero BD, Eggler AL, Mesecar A, Halkides CJ Arch Biochem Biophys. 2008 Nov 15;479(2):105-13. Epub 2008 Sep 5. PMID:18801331^[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
↑ McAdams K, Casper ES, Matthew Haas R, Santarsiero BD, Eggler AL, Mesecar A, Halkides CJ. The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides. Arch Biochem Biophys. 2008 Nov 15;479(2):105-13. Epub 2008 Sep 5. PMID:18801331 doi:http://dx.doi.org/10.1016/j.abb.2008.08.019

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/2id7"

@@ Line 1: / Line 1: @@
 ==1.75 A Structure of T87I Phosphono-CheY==
 <StructureSection load='2id7' size='340' side='right' caption='[[2id7]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c4w|1c4w]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2id7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2id7 OCA], [http://pdbe.org/2id7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2id7 RCSB], [http://www.ebi.ac.uk/pdbsum/2id7 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=2id7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2id7 OCA], [http://pdbe.org/2id7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2id7 RCSB], [http://www.ebi.ac.uk/pdbsum/2id7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2id7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2id7" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Chemotaxis protein|Chemotaxis protein]]
 == References ==
 <references/>

2id7

From Proteopedia

Revision as of 08:28, 18 October 2017

1.75 A Structure of T87I Phosphono-CheY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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