期刊
BIOLOGICAL CHEMISTRY
卷 390, 期 11, 页码 1163-1170出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2009.113
关键词
ABC transporter; choline-binding protein; conformational change; membrane transport
资金
- University of Dusseldorf
- Fonds der chemischen Industrie
- Max Planck Institute for terrestrial Microbiology
- University of Marburg
The periplasmic ligand-binding protein ChoX is part of the ABC transport system ChoVWX that imports choline as a nutrient into the soil bacterium Sinorhizobium meliloti. We have recently reported the crystal structures of ChoX in complex with its ligands choline and acetylcholine and the structure of a fully closed but substrate-free state of ChoX. This latter structure revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. We report here the crystal structure of ChoX in an unusual, ligand-free conformation that represents a semi-closed form of ChoX. The analysis revealed a subdomain movement in the N-lobe of ChoX. Comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.
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