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6FM5

Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher Csu pili of Acinetobacter baumannii

Summary for 6FM5
Entry DOI10.2210/pdb6fm5/pdb
DescriptorCsuA/B,CsuA/B,CsuA/B,CsuA/B (2 entities in total)
Functional Keywordsig-like fold, beta sandwich, donor-strand complementation, cell adhesion
Biological sourceAcinetobacter baumannii
More
Total number of polymer chains1
Total formula weight17643.28
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 citationPakharukova, 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: 30228191
DOI: 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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