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2c9c
From Proteopedia
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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 ... [(full description)]
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 Tue Oct 30 13:04:13 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
