1i5n

From Proteopedia

(Difference between revisions)

Revision as of 10:44, 27 September 2017

Crystal structure of the P1 domain of CheA from Salmonella typhimurium

Structural highlights

1i5n is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CHEA_SALTY] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.

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 x-ray crystal structure of the P1 or H domain of the Salmonella CheA protein has been solved at 2.1-A resolution. The structure is composed of an up-down up-down four-helix bundle that is typical of histidine phosphotransfer or HPt domains such as Escherichia coli ArcB(C) and Saccharomyces cerevisiae Ypd1. Loop regions and additional structural features distinguish all three proteins. The CheA domain has an additional C-terminal helix that lies over the surface formed by the C and D helices. The phosphoaccepting His-48 is located at a solvent-exposed position in the middle of the B helix where it is surrounded by several residues that are characteristic of other HPt domains. Mutagenesis studies indicate that conserved glutamate and lysine residues that are part of a hydrogen-bond network with His-48 are essential for the ATP-dependent phosphorylation reaction but not for the phosphotransfer reaction with CheY. These results suggest that the CheA-P1 domain may serve as a good model for understanding the general function of HPt domains in complex two-component phosphorelay systems.

Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis.,Mourey L, Da Re S, Pedelacq JD, Tolstykh T, Faurie C, Guillet V, Stock JB, Samama JP J Biol Chem. 2001 Aug 17;276(33):31074-82. Epub 2001 May 31. PMID:11387324^[1]

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

References

↑ Mourey L, Da Re S, Pedelacq JD, Tolstykh T, Faurie C, Guillet V, Stock JB, Samama JP. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J Biol Chem. 2001 Aug 17;276(33):31074-82. Epub 2001 May 31. PMID:11387324 doi:10.1074/jbc.M101943200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i5n"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the P1 domain of CheA from Salmonella typhimurium==
 <StructureSection load='1i5n' size='340' side='right' caption='[[1i5n]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1i5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5n OCA], [http://pdbe.org/1i5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i5n RCSB], [http://www.ebi.ac.uk/pdbsum/1i5n 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=1i5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5n OCA], [http://pdbe.org/1i5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i5n RCSB], [http://www.ebi.ac.uk/pdbsum/1i5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5n ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1i5n ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1i5n

From Proteopedia

Revision as of 10:44, 27 September 2017

Crystal structure of the P1 domain of CheA from Salmonella typhimurium

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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