Crystal structure of the ATP-binding subunit of an ABC transporter

• Published in: Nature (London) Vol. 396; no. 6712; pp. 703 - 707
• Main Authors: Kim, Sung-Hou, Hung, Li-Wei, Wang, Iris Xiaoyan, Nikaido, Kishiko, Liu, Pei-Qi, Ames, Giovanna Ferro-Luzzi
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 17.12.1998; Nature Publishing Group
• Subjects: Adenosine Triphosphate - metabolism; Amino Acid Sequence; Amino Acid Transport Systems, Basic; ATP; ATP-Binding Cassette Transporters - chemistry; ATP-Binding Cassette Transporters - metabolism; Bacteria; Bacterial Proteins; Binding Sites; Biological and medical sciences; Cellular biology; Crystalline structure; Crystallography; Crystallography, X-Ray; Cystic Fibrosis Transmembrane Conductance Regulator - chemistry; Drug resistance; E coli; Escherichia coli; Fundamental and applied biological sciences. Psychology; Humans; Membrane Transport Proteins - chemistry; Membrane Transport Proteins - metabolism; Membranes; Models, Molecular; Molecular biophysics; Molecular Sequence Data; Protein Conformation; Proteins; Salmonella typhimurium; Salmonella typhimurium - chemistry; Salmonella typhimurium - enzymology; Sequence Homology, Amino Acid; Structure in molecular biology; Translocation; Membrane protein; Enzyme; Biological transport; Bacteria; Subunit; Salmonella typhimurium; Membrane translocation; Enterobacteriaceae; Structural analysis; Crystalline structure
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/25393

ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety ofcompounds 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 Å 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.