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TitleConformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 3839, Year 2025
Publish dateApr 24, 2025
AuthorsIan Y Yen / Gregory B Whitfield / John L Rubinstein / Lori L Burrows / Yves V Brun / P Lynne Howell /
PubMed AbstractThe type IV pilus family uses PilT/VirB11-like ATPases to rapidly assemble and disassemble pilin subunits. Among these, the tight adherence (Tad) pilus performs both functions using a single ...The type IV pilus family uses PilT/VirB11-like ATPases to rapidly assemble and disassemble pilin subunits. Among these, the tight adherence (Tad) pilus performs both functions using a single bifunctional ATPase, CpaF. Here, we determine three conformationally distinct structures of CpaF hexamers with varying nucleotide occupancies by cryo-electron microscopy. Analysis of these structures suggest ATP binding and hydrolysis expand and rotate the hexamer pore clockwise while subsequent ADP release contracts the ATPase. Truncation of the intrinsically disordered region of CpaF in Caulobacter crescentus equally reduces pilus extension and retraction events observed using fluorescence microscopy, but does not reduce ATPase activity. AlphaFold3 modeling suggests that CpaF and other motors of the type IV filament superfamily employ conserved secondary structural features to engage their respective platform proteins. From these data, we propose that CpaF uses a clockwise, rotary mechanism of catalysis to assemble a right-handed, helical Tad pilus, a process broadly applicable to other single motor systems.
External linksNat Commun / PubMed:40268890 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 4.1 Å
Structure data

EMDB-47431: Consensus map of the CpaF closed structure without nucleotides (Apo dataset)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-47432: Local refined map of the asymmetric unit of the CpaF closed structure without nucleotides (Apo dataset)
Method: EM (single particle) / Resolution: 4.0 Å

47433

9e24

EMDB-47433, PDB-9e24:
Closed structure of CpaF without nucleotides (Apo dataset)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-47434: Consensus map of the CpaF compact structure without nucleotides (Apo dataset)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-47435: Local refined map of the asymmetric unit of the CpaF compact structure without nucleotides (Apo dataset)
Method: EM (single particle) / Resolution: 4.1 Å

47436

9e25

EMDB-47436, PDB-9e25:
Compact structure of CpaF without nucleotides (Apo dataset)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-47437: Consensus map of the CpaF compact structure with two ATPs and two ADPs (Under-saturated ATP/ADP dataset)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-47438: Local refinement of the asymmetric unit of the CpaF compact structure with two ATPs and two ADPs (Under-saturated ATP/ADP dataset)
Method: EM (single particle) / Resolution: 3.2 Å

47439

9e26

EMDB-47439, PDB-9e26:
Compact structure of CpaF with two ATPs and two ADPs (Under-saturated ATP/ADP dataset)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-47440: Consensus map of the CpaF expanded structure with two ATPs and four ADPs (Under-saturated ATP/ADP dataset)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-47441: Local refined map of the asymmetric unit of the CpaF expanded structure with two ATPs and four ADPs (Under-saturated ATP/ADP dataset)
Method: EM (single particle) / Resolution: 3.6 Å

47442

9e27

EMDB-47442, PDB-9e27:
Expanded structure of CpaF with two ATPs and four ADPs (Under-saturated ATP/ADP dataset)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-47444: Consensus map of the CpaF expanded structure with two ATPs and four ADPs (Saturated ATP dataset)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-47445: Local refined map of the asymmetric unit of the CpaF expanded structure with two ATPs and four ADPs (Saturated ATP dataset)
Method: EM (single particle) / Resolution: 3.7 Å

47446

9e29

EMDB-47446, PDB-9e29:
Expanded structure of CpaF with two ATPs and four ADPs (Saturated ATP dataset)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • caulobacter vibrioides (bacteria)
KeywordsMOTOR PROTEIN / ATPase

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