PMID:9872322
| Citation |
Hung, LW, Wang, IX, Nikaido, K, Liu, PQ, Ames, GF and Kim, SH (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396:703-7 |
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| Abstract |
ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety of compounds across membranes of both prokaryotes and eukaryotes. The recently completed Escherichia coli genome sequence revealed that the largest family of paralogous E. coli proteins is composed of ABC transporters. Many eukaryotic proteins of medical significance belong to this family, such as the cystic fibrosis transmembrane conductance regulator (CFTR), the P-glycoprotein (or multidrug-resistance protein) and the heterodimeric transporter associated with antigen processing (Tap1-Tap2). Here we report the crystal structure at 1.5 A resolution of HisP, the ATP-binding subunit of the histidine permease, which is an ABC transporter from Salmonella typhimurium. We correlate the details of this structure with the biochemical, genetic and biophysical properties of the wild-type and several mutant HisP proteins. The structure provides a basis for understanding properties of ABC transporters and of defective CFTR proteins. |
| Links |
PubMed Online version:10.1038/25393 |
| Keywords |
ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Amino Acid Transport Systems, Basic; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry; Humans; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Salmonella typhimurium/chemistry; Salmonella typhimurium/enzymology; Sequence Homology, Amino Acid |
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