期刊
STRUCTURE
卷 15, 期 3, 页码 363-376出版社
CELL PRESS
DOI: 10.1016/j.str.2007.01.018
关键词
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资金
- NCRR NIH HHS [P41 RR007707] Funding Source: Medline
- NIGMS NIH HHS [GM59721, R01 GM059721] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR007707] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM059721] Funding Source: NIH RePORTER
PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 angstrom resolution show N-terminal PAS-like and C-terminal RecA-like ATPase domains followed by a set of short C-terminal helices. The hexamer is formed by extensive polar subunit interactions between the ATPase core of one monomer and the N-terminal domain of the next. An additional structure captures a nonsymmetric PilT hexamer in which approach of invariant arginines from two subunits to the bound nucleotide forms an enzymatically competent active site. A panel of pilT mutations highlights the importance of the arginines, the PAS-like domain, the polar subunit interface, and the C-terminal helices for retraction. We present a model for ATP binding leading to dramatic PilT domain motions, engagement of the arginine wire, and subunit communication in this hexameric motor. Our conclusions apply to the entire type II/IV secretion ATPase family.
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