8RKL
TadA/CpaF nucleotide free
Summary for 8RKL
| Entry DOI | 10.2210/pdb8rkl/pdb |
| EMDB information | 19279 |
| Descriptor | Pilus assembly ATPase CpaF, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (2 entities in total) |
| Functional Keywords | secretion, atpase, apo, motor protein |
| Biological source | Caulobacter vibrioides NA1000 |
| Total number of polymer chains | 6 |
| Total formula weight | 279744.41 |
| Authors | |
| Primary citation | Hohl, M.,Banks, E.J.,Manley, M.P.,Le, T.B.K.,Low, H.H. Bidirectional pilus processing in the Tad pilus system motor CpaF. Nat Commun, 15:6635-6635, 2024 Cited by PubMed Abstract: The bacterial tight adherence pilus system (TadPS) assembles surface pili essential for adhesion and colonisation in many human pathogens. Pilus dynamics are powered by the ATPase CpaF (TadA), which drives extension and retraction cycles in Caulobacter crescentus through an unknown mechanism. Here we use cryogenic electron microscopy and cell-based light microscopy to characterise CpaF mechanism. We show that CpaF assembles into a hexamer with C2 symmetry in different nucleotide states. Nucleotide cycling occurs through an intra-subunit clamp-like mechanism that promotes sequential conformational changes between subunits. Moreover, a comparison of the active sites with different nucleotides bound suggests a mechanism for bidirectional motion. Conserved CpaF residues, predicted to interact with platform proteins CpaG (TadB) and CpaH (TadC), are mutated in vivo to establish their role in pilus processing. Our findings provide a model for how CpaF drives TadPS pilus dynamics and have broad implications for how other ancient type 4 filament family members power pilus assembly. PubMed: 39103374DOI: 10.1038/s41467-024-50280-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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