The ATPase Motor Turns for Type IV Pilus Assembly

Chi-Lin Tsai; John A Tainer

doi:10.1016/j.str.2016.10.002

The ATPase Motor Turns for Type IV Pilus Assembly

Structure. 2016 Nov 1;24(11):1857-1859. doi: 10.1016/j.str.2016.10.002.

Authors

Chi-Lin Tsai¹, John A Tainer²

Affiliations

¹ Department of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, TX 77030, USA.
² Department of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, TX 77030, USA; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: jtainer@mdanderson.org.

PMID: 27806257
DOI: 10.1016/j.str.2016.10.002

Abstract

In this issue of Structure, Mancl et al. (2016) elucidate the crystal structure of the PilB ATPase domain in complex with ATPγS and unveil how ATP binding and hydrolysis coordinates conformational change. Their results reveal a distinct symmetric rotary mechanism for ATP hydrolysis to power bacterial pilus assembly.

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Comment

MeSH terms

Adenosine Triphosphatases / analysis*
Adenosine Triphosphate / analysis
Bacterial Proteins / analysis*
Fimbriae, Bacterial / chemistry
Protein Structure, Secondary

Substances

Bacterial Proteins
Adenosine Triphosphate
Adenosine Triphosphatases