Maloney P C
Department of Physiology, Johns Hopkins Medical School, Baltimore, MD 21205.
Curr Opin Cell Biol. 1994 Aug;6(4):571-82. doi: 10.1016/0955-0674(94)90079-5.
Recent experiments in bacterial systems have established an extended database of sequences broadly relevant to all membrane transporters, allowing serious study of evolutionary relationships. The database will be especially useful in integrating conclusions derived from work with proteins in the major facilitator superfamily, because this kinship includes both eukaryotic and prokaryotic model systems. Even among carriers not linked by evolution, clear hints of functional homology have been note. Advances are also evident in the structural analysis of membrane carriers. Site-directed mutagenesis in a bacterial antiporter has shown how the translocation pathway might be identified; this should complement recent progress in preparing two-dimensional crystals of the eukaryotic anion-exchange protein, band 3. Together, these studies could soon verify or reject the idea that the transport pathway lies at the interface between the amino-terminal and carboxy-terminal helical bundles found in the hydrophobic core of most carrier proteins. If verified, the argument might allow construction of informed three-dimensional models in the absence of crystallographic evidence.
