10NB

Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 4

Summary for 10NB

• Entry DOI: 10.2210/pdb10nb/pdb
• EMDB information: 75299
• Descriptor: PilT/PilU family type 4a pilus ATPase (1 entity in total)
• Functional Keywords: retraction atpase, structural genomics, center for structural biology of infectious diseases, csbid, motor protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 6
• Total formula weight: 257699.11

Authors

Guo, Y.,Shulka, S.,Klose, T.,Tokars, V.,Mondragon, A.,Borek, D.,Satchell, K.,Center for Structural Biology of Infectious Diseases (CSBID) (deposition date: 2026-01-28, release date: 2026-05-20)

Primary citation

Guo, Y.,Shukla, S.,Minasov, G.,Inniss, N.L.,Klose, T.,Tokars, V.L.,Mondragon, A.,Otwinowski, Z.,Borek, D.,Satchell, K.J.F.
Analysis of the heterogenous structural states of the hexameric ATPase PilU of the type IV pili from Vibrio cholerae.
Protein Sci., 35:e70609-e70609, 2026

PubMed Abstract: Type IV pili (T4P) mediate surface motility, host interactions, and DNA uptake through cycles of extension and retraction. While the primary retraction ATPase PilT has been extensively characterized, its homolog PilU remains less well understood despite being demonstrated as a PilT-dependent retraction ATPase. Here, we determined six PilU structures by cryo-electron microscopy and x-ray crystallography. The structures reveal a homohexameric assembly stabilized by interactions between the C-terminal catalytic domain of one subunit and the N-terminal PAS-like domain of a neighboring subunit. PilU adopts multiple conformational states, exhibiting different combinations of open and closed interfaces even in the absence of nucleotide. Comparison with PilT highlights structural features that likely underlie PilU's weak ATPase activity and its dependence on PilT for function. Together, these findings provide a structural framework for understanding PilU's role within the T4P retraction machinery.

PubMed: 42084485
DOI: 10.1002/pro.70609

Experimental method

ELECTRON MICROSCOPY (3.76 Å)