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9Q6M

Crystal Structure of Vibrio cholerae PilU, a PilT-dependent Retraction ATPase - Crystal Form 1.

Summary for 9Q6M
Entry DOI10.2210/pdb9q6m/pdb
DescriptorTwitching motility protein PilT (2 entities in total)
Functional Keywordsstructural genomics, center for structural biology of infectious diseases, csbid, pilu, pilt-dependent retraction atpase, motor protein
Biological sourceVibrio cholerae O1 biovar El Tor str. N16961
Total number of polymer chains6
Total formula weight257699.11
Authors
Minasov, G.,Shukla, S.,Shuvalova, L.,Brunzelle, J.S.,Satchell, K.J.F.,Center for Structural Biology of Infectious Diseases (CSBID) (deposition date: 2025-08-22, release date: 2026-05-20, Last modification date: 2026-06-03)
Primary citationGuo, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.95 Å)
Structure validation

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