10my

Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 1

spinqualitylabelsall models 10my, resolution 3.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 10my is a 6 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.44Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Analysis of the heterogenous structural states of the hexameric ATPase PilU of the type IV pili from Vibrio cholerae.,Guo Y, Shukla S, Minasov G, Inniss NL, Klose T, Tokars VL, Mondragon A, Otwinowski Z, Borek D, Satchell KJF Protein Sci. 2026 Jun;35(6):e70609. doi: 10.1002/pro.70609. PMID:42084485 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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