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Published Online August 2, 2007
Science DOI: 10.1126/science.1145950

Reports

Submitted on June 4, 2007
Accepted on July 19, 2007

Asymmetry in the Structure of the ABC Transporter–Binding Protein Complex BtuCD-BtuF

Rikki N. Hvorup 1, Birke A. Goetz 1, Martina Niederer 1, Kaspar Hollenstein 1, Eduardo Perozo 2, Kaspar P. Locher 1*

1 Institute of Molecular Biology and Biophysics, ETH Zurich HPK D14.3, 8093 Zurich, Switzerland.
2 nstitute of Molecular Pediatric Science and Department of Biochemistry and Molecular Biology, University of Chicago, 929 East 57th Street, CIS W206, Chicago, IL 60637, USA.

* To whom correspondence should be addressed.
Kaspar P. Locher , E-mail: kaspar.locher{at}mol.biol.ethz.ch

BtuCD is an ABC transporter that translocates vitamin B12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 Å crystal structure of a complex BtuCD-F reveals substantial conformational changes compared to the previously reported structures of BtuCD and of BtuF. The lobes of BtuF are spread apart and B12 is displaced from the binding pocket. The transmembrane BtuC subunits reveal two distinct conformations, and the translocation pathway is closed to both sides of the membrane. Electron paramagnetic resonance spectra of spin-labeled cysteine mutants reconstituted in proteoliposomes are consistent with the conformation of BtuCD-F as observed in the crystal structure. Comparison with BtuCD and the homologous HI1470/71 protein suggests that the structure of BtuCD-F may reflect a post-translocation intermediate.


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