5IT5

Thermus thermophilus PilB core ATPase region

5IT5 の概要

• エントリーDOI: 10.2210/pdb5it5/pdb
• 分子名称: ATP binding motif-containing protein PilF, ZINC ION, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: atpase, aaa+, hexamer, type iv pilus, transport protein
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 258726.43

構造登録者

Mancl, J.,Robinson, H.,Black, W.,Yang, Z.,Schubot, F. (登録日: 2016-03-16, 公開日: 2016-10-19, 最終更新日: 2023-09-27)

主引用文献

Mancl, J.M.,Black, W.P.,Robinson, H.,Yang, Z.,Schubot, F.D.
Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus.
Structure, 24:1886-1897, 2016

PubMed Abstract: Type IV pili (T4P) mediate bacterial motility and virulence. The PilB/GspE family ATPases power the assembly of T4P and type 2 secretion systems. We determined the structure of the ATPase region of PilB (PilB) in complex with ATPγS to provide a model of a T4P assembly ATPase and a view of a PilB/GspE family hexamer at better than 3-Å resolution. Spatial positioning and conformations of the protomers suggest a mechanism of force generation. All six PilB protomers contain bound ATPγS. Two protomers form a closed conformation poised for ATP hydrolysis. The other four molecules assume an open conformation but separate into two pairs with distinct active-site accessibilities. We propose that one pair represents the post-hydrolysis phase while the other pair appears poised for ADP/ATP exchange. Collectively, the data suggest that T4P assembly is powered by coordinating concurrent substrate binding with ATP hydrolysis across the PilB hexamer.

PubMed: 27667690
DOI: 10.1016/j.str.2016.08.010

実験手法

X-RAY DIFFRACTION (2.648 Å)