6OLL

CryoEM structure of PilT4 from Geobacter metallireducens without adding nucleotide: C2oocooc conformation

6OLL の概要

• エントリーDOI: 10.2210/pdb6oll/pdb
• 関連するPDBエントリー: 6OJX 6OJY 6OJZ 6OK2 6OKV
• EMDBエントリー: 20116
• 分子名称: Twitching motility pilus retraction ATPase (1 entity in total)
• 機能のキーワード: atpase, t4p, type iv pilus, motor, motor 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: 6
• 化学式量合計: 257300.27

構造登録者

McCallum, M.,Howell, P.L. (登録日: 2019-04-16, 公開日: 2019-11-20, 最終更新日: 2024-03-20)

主引用文献

McCallum, M.,Benlekbir, S.,Nguyen, S.,Tammam, S.,Rubinstein, J.L.,Burrows, L.L.,Howell, P.L.
Multiple conformations facilitate PilT function in the type IV pilus.
Nat Commun, 10:5198-5198, 2019

PubMed Abstract: Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by motor ATPases of the PilT/VirB11-like family. This family is thought to operate with C symmetry; however, most of these ATPases crystallize with either C or C symmetric conformations. The relevance of these conformations is unclear. Here, we determine the X-ray structures of PilT in four unique conformations and use these structures to classify the conformation of available PilT/VirB11-like family member structures. Single particle electron cryomicroscopy (cryoEM) structures of PilT reveal condition-dependent preferences for C C, and C conformations. The physiologic importance of these conformations is validated by coevolution analysis and functional studies of point mutants, identifying a rare gain-of-function mutation that favours the C conformation. With these data, we propose a comprehensive model of PilT function with broad implications for PilT/VirB11-like family members.

PubMed: 31729381
DOI: 10.1038/s41467-019-13070-z

実験手法

ELECTRON MICROSCOPY (4.1 Å)