6FM5
Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher Csu pili of Acinetobacter baumannii
Summary for 6FM5
| Entry DOI | 10.2210/pdb6fm5/pdb |
| Descriptor | CsuA/B,CsuA/B,CsuA/B,CsuA/B (2 entities in total) |
| Functional Keywords | ig-like fold, beta sandwich, donor-strand complementation, cell adhesion |
| Biological source | Acinetobacter baumannii More |
| Total number of polymer chains | 1 |
| Total formula weight | 17643.28 |
| Authors | Pakharukova, N.A.,Tuitilla, M.,Paavilainen, S.,Zavialov, A.V. (deposition date: 2018-01-30, release date: 2018-09-26, Last modification date: 2024-11-20) |
| Primary citation | Pakharukova, N.,McKenna, S.,Tuittila, M.,Paavilainen, S.,Malmi, H.,Xu, Y.,Parilova, O.,Matthews, S.,Zavialov, A.V. Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information. J. Biol. Chem., 293:17070-17080, 2018 Cited by PubMed Abstract: Adhesive pili are external component of fibrous adhesive organelles and help bacteria attach to biotic or abiotic surfaces. The biogenesis of adhesive pili via the chaperone-usher pathway (CUP) is independent of external energy sources. In the classical CUP, chaperones transport assembly-competent pilins in a folded but expanded conformation. During donor-strand exchange, pilins subsequently collapse, producing a tightly packed hydrophobic core and releasing the necessary free energy to drive fiber formation. Here, we show that pilus biogenesis in non-classical, archaic, and alternative CUPs uses a different source of conformational energy. High-resolution structures of the archaic Csu-pili system from revealed that non-classical chaperones employ a short donor strand motif that is insufficient to fully complement the pilin fold. This results in chaperone-bound pilins being trapped in a substantially unfolded intermediate. The exchange of this short motif with the longer donor strand from adjacent pilin provides the full steric information essential for folding, and thereby induces a large unfolded-to-folded conformational transition to drive assembly. Our findings may inform the development of anti-adhesion drugs (pilicides) to combat bacterial infections. PubMed: 30228191DOI: 10.1074/jbc.RA118.004170 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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