PDBsum entry 6olm

Motor protein

PDB id: 6olm

Contents

Protein chains

(+ 0 more) 352 a.a.

Ligands

ATP ×6

PDB id:

6olm

Name:

Motor protein

Title:

Cryoem structure of pilt4 from geobacter metallireducens with added atp: c6cccccc conformation

Structure:

Twitching motility pilus retraction atpase. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Geobacter metallireducens (strain gs-15 / atcc 53774 / dsm 7210). Organism_taxid: 269799. Strain: gs-15 / atcc 53774 / dsm 7210. Gene: pilt-4, gmet_1394. Expressed in: escherichia coli. Expression_system_taxid: 562.

Authors:

M.Mccallum,P.L.Howell

Key ref:

M.McCallum et al. (2019). Multiple conformations facilitate PilT function in the type IV pilus. Nat Commun, 10, 5198. PubMed id: 31729381 DOI: 10.1038/s41467-019-13070-z

Date:

16-Apr-19 Release date: 20-Nov-19

Protein chains

Q39VU6  (Q39VU6_GEOMG) -  Twitching motility pilus retraction ATPase from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)

Seq: 365 a.a.

Struc: 352 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/s41467-019-13070-z

Nat Commun 10:5198 (2019)

PubMed id: 31729381

Multiple conformations facilitate PilT function in the type IV pilus.

M.McCallum, S.Benlekbir, S.Nguyen, S.Tammam, J.L.Rubinstein, L.L.Burrows, P.L.Howell.

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 C₂ symmetry; however, most of these ATPases crystallize with either C₃ or C₆ 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_2, C₃, and C₆ 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 C₂ conformation. With these data, we propose a comprehensive model of PilT function with broad implications for PilT/VirB11-like family members.