2c98: Difference between revisions
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==Overview== | ==Overview== | ||
Bacterial enhancer-binding proteins (EBP) activate transcription by, hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter, complex. We compare six high resolution structures (<2.1 A) of the AAA(+), domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the, atomic details underpinning the origins of the conformational changes, occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain, respond distinctively to nucleotide binding and hydrolysis, suggesting, functional roles during the hydrolysis cycle, which completely agree with, those derived from activities of PspF mutated at these positions. We, propose a putative atomic switch that is responsible for coupling, structural . | Bacterial enhancer-binding proteins (EBP) activate transcription by, hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter, complex. We compare six high resolution structures (<2.1 A) of the AAA(+), domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the, atomic details underpinning the origins of the conformational changes, occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain, respond distinctively to nucleotide binding and hydrolysis, suggesting, functional roles during the hydrolysis cycle, which completely agree with, those derived from activities of PspF mutated at these positions. We, propose a putative atomic switch that is responsible for coupling, structural changes in the nucleotide-binding site to the repositioning of, the sigma(54)-interacting loops. Striking similarities in, nucleotide-specific conformational changes and atomic switch exist between, PspF and the large T antigen helicase, suggesting conservation in the, origin of those events amongst AAA(+) proteins. | ||
==About this Structure== | ==About this Structure== | ||
2C98 is a | 2C98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C98 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: two-component regulatory system]] | [[Category: two-component regulatory system]] | ||
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Revision as of 15:20, 5 November 2007
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STRUCTURAL BASIS OF THE NUCLEOTIDE DRIVEN CONFORMATIONAL CHANGES IN THE AAA DOMAIN OF TRANSCRIPTION ACTIVATOR PSPF
OverviewOverview
Bacterial enhancer-binding proteins (EBP) activate transcription by, hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter, complex. We compare six high resolution structures (<2.1 A) of the AAA(+), domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the, atomic details underpinning the origins of the conformational changes, occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain, respond distinctively to nucleotide binding and hydrolysis, suggesting, functional roles during the hydrolysis cycle, which completely agree with, those derived from activities of PspF mutated at these positions. We, propose a putative atomic switch that is responsible for coupling, structural changes in the nucleotide-binding site to the repositioning of, the sigma(54)-interacting loops. Striking similarities in, nucleotide-specific conformational changes and atomic switch exist between, PspF and the large T antigen helicase, suggesting conservation in the, origin of those events amongst AAA(+) proteins.
About this StructureAbout this Structure
2C98 is a Single protein structure of sequence from Escherichia coli with ADP as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF., Rappas M, Schumacher J, Niwa H, Buck M, Zhang X, J Mol Biol. 2006 Mar 24;357(2):481-92. Epub 2006 Jan 13. PMID:16430918
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