Solutes modify a conformational transition in a membrane transport protein.

ABSTRACT: The bacterial outer-membrane vitamin B(12) transporter, BtuB, undergoes a dramatic order-to-disorder transition in its N-terminal energy-coupling motif (Ton box) upon substrate binding. Here, site-directed spin labeling (SDSL) is used to show that a range of solutes prevents this conformational change when ligand is bound to BtuB, resulting in a more ordered Ton box structure. For each solute examined, the data indicate that solutes effectively block this conformational transition through an osmotic mechanism. The molecular weight dependence of this solute effect has been examined for a series of polyethylene glycols, and a sharp molecular weight cutoff is observed. This cutoff indicates that solutes are preferentially excluded from a cavity within the protein as well as the protein surfac

SUBMITTER: Kim M 

PROVIDER: S-EPMC1414566 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature