Literature DB >> 18023171

The AAA+ superfamily--a myriad of motions.

Paul A Tucker1, László Sallai.   

Abstract

ATPases associated with various cellular activities are aptly named. They are the engines that drive processes such as protein degradation, protein refolding, sigma(54)-dependent transcriptional activation, DNA helicase activity, DNA replication initiation, and cellular cargo transport. Recent structural information derived from biochemical studies, electron microscopy (EM), small-angle X-ray scattering (SAXS), and X-ray crystallography are beginning to show how, at an atomic level, some of these systems use the conformational changes generated during the ATP hydrolysis cycle. Structural highlights in the processes mentioned are provided by work on ClpX and p97, ClpB, PspF and NtrC, RuvBL1, DnaA and the papillomavirus E1 initiator protein and dynein. The results emphasize the versatility of the AAA+ core domain.

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Year:  2007        PMID: 18023171     DOI: 10.1016/j.sbi.2007.09.012

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  49 in total

1.  Simulations of the p97 complex suggest novel conformational states of hydrolysis intermediates.

Authors:  Jeff Wereszczynski; J Andrew McCammon
Journal:  Protein Sci       Date:  2012-03-02       Impact factor: 6.725

2.  Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA.

Authors:  Graham Scholefield; Jeff Errington; Heath Murray
Journal:  EMBO J       Date:  2012-01-27       Impact factor: 11.598

3.  The 2.8 Å crystal structure of the dynein motor domain.

Authors:  Takahide Kon; Takuji Oyama; Rieko Shimo-Kon; Kenji Imamula; Tomohiro Shima; Kazuo Sutoh; Genji Kurisu
Journal:  Nature       Date:  2012-03-07       Impact factor: 49.962

4.  Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.

Authors:  Karin Walldén; Robert Williams; Jun Yan; Pei W Lian; Luchun Wang; Konstantinos Thalassinos; Elena V Orlova; Gabriel Waksman
Journal:  Proc Natl Acad Sci U S A       Date:  2012-06-27       Impact factor: 11.205

5.  A prehydrolysis state of an AAA+ ATPase supports transcription activation of an enhancer-dependent RNA polymerase.

Authors:  Patricia C Burrows; Nicolas Joly; Martin Buck
Journal:  Proc Natl Acad Sci U S A       Date:  2010-05-03       Impact factor: 11.205

6.  Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase.

Authors:  Baoyu Chen; Tatyana A Sysoeva; Saikat Chowdhury; Liang Guo; Sacha De Carlo; Jeffrey A Hanson; Haw Yang; B Tracy Nixon
Journal:  Structure       Date:  2010-11-10       Impact factor: 5.006

7.  Crystallization and preliminary X-ray analysis of the ATPase domain of the σ(54)-dependent transcription activator NtrC1 from Aquifex aeolicus bound to the ATP analog ADP-BeFx.

Authors:  Tatyana A Sysoeva; Neela Yennawar; Marc Allaire; B Tracy Nixon
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-11-29

8.  Paddling mechanism for the substrate translocation by AAA+ motor revealed by multiscale molecular simulations.

Authors:  Nobuyasu Koga; Tomoshi Kameda; Kei-ichi Okazaki; Shoji Takada
Journal:  Proc Natl Acad Sci U S A       Date:  2009-10-14       Impact factor: 11.205

9.  Single chain forms of the enhancer binding protein PspF provide insights into geometric requirements for gene activation.

Authors:  Nicolas Joly; Martin Buck
Journal:  J Biol Chem       Date:  2011-02-07       Impact factor: 5.157

10.  YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity.

Authors:  Feng Rao; Rui Yin See; Dongwei Zhang; Delon Chengxu Toh; Qiang Ji; Zhao-Xun Liang
Journal:  J Biol Chem       Date:  2009-11-09       Impact factor: 5.157

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