5TSG

PilB from Geobacter metallireducens bound to ADP

5TSG の概要

• エントリーDOI: 10.2210/pdb5tsg/pdb
• 関連するPDBエントリー: 5TSH
• 分子名称: Type IV pilus biogenesis ATPase PilB, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: pilb, pilus, type iva pilus, extension, atp-binding protein
• 由来する生物種: Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 195801.01

構造登録者

McCallum, M.,Tammam, S.,Khan, A.,Burrows, L.,Howell, P.L. (登録日: 2016-10-28, 公開日: 2017-05-17, 最終更新日: 2023-10-04)

主引用文献

McCallum, M.,Tammam, S.,Khan, A.,Burrows, L.L.,Howell, P.L.
The molecular mechanism of the type IVa pilus motors.
Nat Commun, 8:15091-15091, 2017

PubMed Abstract: Type IVa pili are protein filaments essential for virulence in many bacterial pathogens; they extend and retract from the surface of bacterial cells to pull the bacteria forward. The motor ATPase PilB powers pilus assembly. Here we report the structures of the core ATPase domains of Geobacter metallireducens PilB bound to ADP and the non-hydrolysable ATP analogue, AMP-PNP, at 3.4 and 2.3 Å resolution, respectively. These structures reveal important differences in nucleotide binding between chains. Analysis of these differences reveals the sequential turnover of nucleotide, and the corresponding domain movements. Our data suggest a clockwise rotation of the central sub-pores of PilB, which through interactions with PilC, would support the assembly of a right-handed helical pilus. Our analysis also suggests a counterclockwise rotation of the C2 symmetric PilT that would enable right-handed pilus disassembly. The proposed model provides insight into how this family of ATPases can power pilus extension and retraction.

PubMed: 28474682
DOI: 10.1038/ncomms15091

実験手法

X-RAY DIFFRACTION (3.4011 Å)