2c9c
From Proteopedia
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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== | ||
| - | 2C9C is a | + | 2C9C 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 MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two-component regulatory system]] | [[Category: two-component regulatory system]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:26:13 2007'' |
Revision as of 12:20, 5 November 2007
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STRUCTURAL BASIS OF THE NUCLEOTIDE DRIVEN CONFORMATIONAL CHANGES IN THE AAA DOMAIN OF TRANSCRIPTION ACTIVATOR PSPF
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 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
2C9C is a Single protein structure of sequence from Escherichia coli with MG and ATP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 14:26:13 2007
Categories: Escherichia coli | Single protein | Buck, M. | Niwa, H. | Rappas, M. | Schumacher, J. | Zhang, X. | ATP | MG | Aaa domain | Activator | Atp-binding | Atpase | Bacterial sigma54 activator | Dna-binding | Nucleotide-binding | Sensory transduction | Transcription regulation | Two-component regulatory system
