2chf

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{{STRUCTURE_2chf| PDB=2chf | SCENE= }}
{{STRUCTURE_2chf| PDB=2chf | SCENE= }}
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'''STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS'''
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===STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8257674}}
==About this Structure==
==About this Structure==
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[[Category: West, A.]]
[[Category: West, A.]]
[[Category: Signal transduction protein]]
[[Category: Signal transduction protein]]
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Revision as of 13:52, 28 July 2008

Image:2chf.png

Template:STRUCTURE 2chf

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

Template:ABSTRACT PUBMED 8257674

About this Structure

2CHF is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

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

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