Article
ATP Ground- and Transition States of Bacterial Enhancer Binding AAA+ ATPases Support Complex Formation with Their Target Protein, σ54
Structure
(2007)
Abstract
Transcription initiation by the σ54 form of bacterial RNA polymerase requires hydrolysis of ATP by an enhancer binding protein (EBP). We present SAS-based solution structures of the ATPase domain of the EBP NtrC1 from Aquifex aeolicus in different nucleotide states. Structures of apo protein and that bound to AMPPNP or ADP-BeFx (ground-state mimics), ADP-AlFx (a transition-state mimic), or ADP (product) show substantial changes in the position of the GAFTGA loops that contact polymerase, particularly upon conversion from the apo state to the ADP-BeFx state, and from the ADP-AlFx state to the ADP state. Binding of the ATP analogs stabilizes the oligomeric form of the ATPase and its binding to σ54, with ADP-AlFx having the largest effect. These data indicate that ATP binding promotes a conformational change that stabilizes complexes between EBPs and σ54, while subsequent hydrolysis and phosphate release drive the conformational change needed to open the polymerase/promoter complex.
Disciplines
Publication Date
April, 2007
Publisher Statement
Copyright © 2007 Elsevier Ltd.
Citation Information
Baoyu Chen, Michaeleen Doucleff, David E. Wemmer, Sacha De Carlo, et al.. "ATP Ground- and Transition States of Bacterial Enhancer Binding AAA+ ATPases Support Complex Formation with Their Target Protein, σ54" Structure Vol. 15 Iss. 4 (2007) p. 429 - 440 Available at: http://works.bepress.com/baoyu-chen/10/
Creative Commons license
This work is licensed under a Creative Commons CC_BY-NC-ND International License.