5D6H
Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii
Summary for 5D6H
| Entry DOI | 10.2210/pdb5d6h/pdb |
| Descriptor | CsuC, CsuA/B (3 entities in total) |
| Functional Keywords | archaic chaperone-usher pathway, ig-like fold, beta sheet sandwich, donor-strand complementation, chaperone-protein transport complex, chaperone/protein transport |
| Biological source | Acinetobacter baumannii More |
| Total number of polymer chains | 2 |
| Total formula weight | 43122.66 |
| Authors | Pakharukova, N.A.,Tuitilla, M.,Paavilainen, S.,Zavialov, A. (deposition date: 2015-08-12, release date: 2015-11-04, Last modification date: 2024-11-13) |
| Primary citation | Pakharukova, N.,Garnett, J.A.,Tuittila, M.,Paavilainen, S.,Diallo, M.,Xu, Y.,Matthews, S.J.,Zavialov, A.V. Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis. Plos Pathog., 11:e1005269-e1005269, 2015 Cited by PubMed Abstract: Gram-negative pathogens express fibrous adhesive organelles that mediate targeting to sites of infection. The major class of these organelles is assembled via the classical, alternative and archaic chaperone-usher pathways. Although non-classical systems share a wider phylogenetic distribution and are associated with a range of diseases, little is known about their assembly mechanisms. Here we report atomic-resolution insight into the structure and biogenesis of Acinetobacter baumannii Csu and Escherichia coli ECP biofilm-mediating pili. We show that the two non-classical systems are structurally related, but their assembly mechanism is strikingly different from the classical assembly pathway. Non-classical chaperones, unlike their classical counterparts, maintain subunits in a substantially disordered conformational state, akin to a molten globule. This is achieved by a unique binding mechanism involving the register-shifted donor strand complementation and a different subunit carboxylate anchor. The subunit lacks the classical pre-folded initiation site for donor strand exchange, suggesting that recognition of its exposed hydrophobic core starts the assembly process and provides fresh inspiration for the design of inhibitors targeting chaperone-usher systems. PubMed: 26587649DOI: 10.1371/journal.ppat.1005269 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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