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ATP Ground- and Transition States of Bacterial Enhancer Binding AAA+ ATPases Support Complex Formation with Their Target Protein, σ54
Structure (2007)
  • Baoyu Chen, The Pennsylvania State University
  • Michaeleen Doucleff, University of California - Berkeley
  • David E. Wemmer, University of California - Berkeley
  • Sacha De Carlo, University of California - Berkeley
  • Hector H. Huang, University of California - Berkeley
  • Eva Nogales, University of California - Berkeley
  • Timothy R. Hoover, University of Georgia
  • Elena Kondrashkina, Illinois Institute of Technology
  • Liang Guo, Illinois Institute of Technology
  • B. Tracy Nixon, The Pennsylvania State University
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.
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
Creative Commons License
This work is licensed under a Creative Commons CC_BY-NC-ND International License.