The ATPase Motor Turns for Type IV Pilus Assembly.
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.
Department of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, TX 77030, USA.
Chi-Lin
CL
Tsai
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.
John A
JA
Tainer
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000255:Adenosine Triphosphate / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis*; D010861:Fimbriae, Bacterial / Q000737:chemistry; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases