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- Title
The structure of BtuB with bound colicin E3 R-domain implies a translocon.
- Authors
Kurisu, Genji; Zakharov, Stanislav D; Zhalnina, Mariya V; Bano, Sufiya; Eroukova, Veronika Y; Rokitskaya, Tatiana I; Antonenko, Yuri N; Wiener, Michael C; Cramer, William A
- Abstract
Cellular import of colicin E3 is initiated by the Escherichia coli outer membrane cobalamin transporter, BtuB. The 135-residue 100-Å coiled-coil receptor-binding domain (R135) of colicin E3 forms a 1:1 complex with BtuB whose structure at a resolution of 2.75 Å is reported. Binding of R135 to the BtuB extracellular surface (?G° = -12 kcal mol-1) is mediated by 27 residues of R135 near the coiled-coil apex. Formation of the R135-BtuB complex results in unfolding of R135 N- and C-terminal ends, inferred to be important for unfolding of the colicin T-domain. Small conformational changes occur in the BtuB cork and barrel domains but are insufficient to form a translocation channel. The absence of a channel and the peripheral binding of R135 imply that BtuB serves to bind the colicin, and that the coiled-coil delivers the colicin to a neighboring outer membrane protein for translocation, thus forming a colicin translocon. The translocator was concluded to be OmpF from the occlusion of OmpF channels by colicin E3.
- Subjects
ESCHERICHIA coli; PLANT translocation; BIOLOGICAL transport; BACTERIOPHAGES; ORGANELLES; PLANT organelles
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 11, p948
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb997