A 3D structure model of the melibiose permease of Escherichia coli represents a distinctive fold for Na+ symporters.

ABSTRACT: The melibiose permease of Escherichia coli (MelB) catalyzes the coupled stoichiometric symport of a galactoside with a cation (either Na(+), Li(+), or H(+)), using free energy from the downhill translocation of one cosubstrate to catalyze the accumulation of the other. Here, we present a 3D structure model of MelB threaded through a crystal structure of the lactose permease of E. coli (LacY), manually adjusted, and energetically minimized. The model contains 442 consecutive residues ( approximately 94% of the polypeptide), including all 12 transmembrane helices and connecting loops, with no steric clashes and superimposes well with the template structure. The electrostatic surface potential calculated from the model is typical for a membrane protein and exhibits a characteristic ring of po

SUBMITTER: Yousef MS 

PROVIDER: S-EPMC2729278 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature