Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 357, Issue 2, Pages 481-492Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2005.12.052
Keywords
AAA(+) ATPase; conformational signaling; sigma(54); transcription activation; crystal structures
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Funding
- Biotechnology and Biological Sciences Research Council [B17129] Funding Source: Medline
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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 angstrom) of the AAA(+) domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg2+-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 PspFs 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. (c) 2005 Elsevier Ltd. All rights reserved.
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