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: 2018-11-14) |
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: 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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