NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA.

ABSTRACT: Structural studies of polytopic membrane proteins are often hampered by the vagaries of these proteins in membrane mimetic environments and by the difficulties in handling them with conventional techniques. Designing and creating water-soluble analogues with preserved native structures offer an attractive alternative. We report here solution NMR studies of WSK3, a water-soluble analogue of the potassium channel KcsA. The WSK3 NMR structure (PDB ID code 2K1E) resembles the KcsA crystal structures, validating the approach. By more stringent comparison criteria, however, the introduction of several charged residues aimed at improving water solubility seems to have led to the possible formations of a few salt bridges and hydrogen bonds not present in the native structure, resulting in slight d

SUBMITTER: Ma D 

PROVIDER: S-EPMC2572164 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature