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.

2chf

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 20:35, 20 October 2021

STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS

Structural highlights

2chf is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CHEY_SALTY] 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. Shows autophosphatase activity which is enhanced by CheZ.

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 response regulator protein of bacterial chemotaxis, CheY, is representative of a large family of signal transduction proteins that function as phosphorylation-activated switches to regulate the activities of associated effector domains. These regulators catalyze the metal ion-dependent phosphoryl transfer and dephosphorylation reactions that control the effector activities. The crystal structures of Salmonella typhimurium CheY with and without Mg2+ bound at the active site have been determined and refined at 1.8-A resolution. While the overall structures of metal-bound and metal-free CheY are similar, significant rearrangements occur within the active site involving the three most highly conserved residues of the response regulator family. Conservation of the cluster of carboxylate side chains at the active site of response regulator domains can be rationalized in terms of their role in coordinating the catalytically essential divalent metal ion. The Mg2+ coordination geometry provides insights to the mechanism of phosphoryl transfer.

Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis.,Stock AM, Martinez-Hackert E, Rasmussen BF, West AH, Stock JB, Ringe D, Petsko GA Biochemistry. 1993 Dec 14;32(49):13375-80. PMID:8257674^[1]

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

References

↑ Stock AM, Martinez-Hackert E, Rasmussen BF, West AH, Stock JB, Ringe D, Petsko GA. Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry. 1993 Dec 14;32(49):13375-80. PMID:8257674

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/2chf"

@@ Line 3: / Line 3: @@
 <StructureSection load='2chf' size='340' side='right'caption='[[2chf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2chf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2chf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHF FirstGlance]. <br>
-</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=2chf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chf OCA], [http://pdbe.org/2chf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2chf RCSB], [http://www.ebi.ac.uk/pdbsum/2chf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2chf ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2chf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chf OCA], [https://pdbe.org/2chf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2chf RCSB], [https://www.ebi.ac.uk/pdbsum/2chf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2chf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CHEY_SALTY CHEY_SALTY]] 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. Shows autophosphatase activity which is enhanced by CheZ.
+[[https://www.uniprot.org/uniprot/CHEY_SALTY CHEY_SALTY]] 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. Shows autophosphatase activity which is enhanced by CheZ.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2chf

From Proteopedia

Revision as of 20:35, 20 October 2021

STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox