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1bdj

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Revision as of 10:57, 8 November 2017

COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY

Structural highlights

1bdj is a 2 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, 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] [ARCB_ECOLI] Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576.

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 structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 A resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.

Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY.,Kato M, Shimizu T, Mizuno T, Hakoshima T Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1257-63. PMID:10393292^[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
↑ Kato M, Shimizu T, Mizuno T, Hakoshima T. Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY. Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1257-63. PMID:10393292

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/1bdj"

@@ Line 1: / Line 1: @@
 ==COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY==
 <StructureSection load='1bdj' size='340' side='right' caption='[[1bdj]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1bdj]] is a 2 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=1BDJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BDJ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1bdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bdj OCA], [http://pdbe.org/1bdj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bdj RCSB], [http://www.ebi.ac.uk/pdbsum/1bdj 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=1bdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bdj OCA], [http://pdbe.org/1bdj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bdj RCSB], [http://www.ebi.ac.uk/pdbsum/1bdj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bdj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1bdj" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Chemotaxis protein|Chemotaxis protein]]
 == References ==
 <references/>

1bdj

From Proteopedia

Revision as of 10:57, 8 November 2017

COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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