2pmc: Difference between revisions
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==Overview== | ==Overview== | ||
Chemotaxis, a means for motile bacteria to sense the environment and | Chemotaxis, a means for motile bacteria to sense the environment and achieve directed swimming, is controlled by flagellar rotation. The primary output of the chemotaxis machinery is the phosphorylated form of the response regulator CheY (P-CheY). The steady-state level of P-CheY dictates the direction of rotation of the flagellar motor. The chemotaxis signal in the form of P-CheY is terminated by the phosphatase CheZ. Efficient dephosphorylation of CheY by CheZ requires two distinct protein-protein interfaces: one involving the strongly conserved C-terminal helix of CheZ (CheZ(C)) tethering the two proteins together and the other constituting an active site for catalytic dephosphorylation. In a previous work (J. Guhaniyogi, V. L. Robinson, and A. M. Stock, J. Mol. Biol. 359:624-645, 2006), we presented high-resolution crystal structures of CheY in complex with the CheZ(C) peptide that revealed alternate binding modes subject to the conformational state of CheY. In this study, we report biochemical and structural data that support the alternate-binding-mode hypothesis and identify key recognition elements in the CheY-CheZ(C) interaction. In addition, we present kinetic studies of the CheZ(C)-associated effect on CheY phosphorylation with its physiologically relevant phosphodonor, the histidine kinase CheA. Our results indicate mechanistic differences in phosphotransfer from the kinase CheA versus that from small-molecule phosphodonors, explaining a modest twofold increase of CheY phosphorylation with the former, observed in this study, relative to a 10-fold increase previously documented with the latter. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
Interaction of CheY with the C- | Interaction of CheY with the C-terminal peptide of CheZ., Guhaniyogi J, Wu T, Patel SS, Stock AM, J Bacteriol. 2008 Feb;190(4):1419-28. Epub 2007 Dec 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18083806 18083806] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Guhaniyogi, J.]] | [[Category: Guhaniyogi, J.]] | ||
[[Category: Stock, A | [[Category: Stock, A M.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:03 2008'' | ||
Revision as of 19:31, 21 February 2008
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Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal
OverviewOverview
Chemotaxis, a means for motile bacteria to sense the environment and achieve directed swimming, is controlled by flagellar rotation. The primary output of the chemotaxis machinery is the phosphorylated form of the response regulator CheY (P-CheY). The steady-state level of P-CheY dictates the direction of rotation of the flagellar motor. The chemotaxis signal in the form of P-CheY is terminated by the phosphatase CheZ. Efficient dephosphorylation of CheY by CheZ requires two distinct protein-protein interfaces: one involving the strongly conserved C-terminal helix of CheZ (CheZ(C)) tethering the two proteins together and the other constituting an active site for catalytic dephosphorylation. In a previous work (J. Guhaniyogi, V. L. Robinson, and A. M. Stock, J. Mol. Biol. 359:624-645, 2006), we presented high-resolution crystal structures of CheY in complex with the CheZ(C) peptide that revealed alternate binding modes subject to the conformational state of CheY. In this study, we report biochemical and structural data that support the alternate-binding-mode hypothesis and identify key recognition elements in the CheY-CheZ(C) interaction. In addition, we present kinetic studies of the CheZ(C)-associated effect on CheY phosphorylation with its physiologically relevant phosphodonor, the histidine kinase CheA. Our results indicate mechanistic differences in phosphotransfer from the kinase CheA versus that from small-molecule phosphodonors, explaining a modest twofold increase of CheY phosphorylation with the former, observed in this study, relative to a 10-fold increase previously documented with the latter.
About this StructureAbout this Structure
2PMC is a Protein complex structure of sequences from Salmonella typhimurium with as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
Interaction of CheY with the C-terminal peptide of CheZ., Guhaniyogi J, Wu T, Patel SS, Stock AM, J Bacteriol. 2008 Feb;190(4):1419-28. Epub 2007 Dec 14. PMID:18083806
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