1B0U

ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM

Summary for 1B0U

• Entry DOI: 10.2210/pdb1b0u/pdb
• Descriptor: HISTIDINE PERMEASE, CHLORIDE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: abc transporter, histidine permease, transport protein
• Biological source: Salmonella typhimurium
• Cellular location: Cell inner membrane; Peripheral membrane protein: P02915
• Total number of polymer chains: 1
• Total formula weight: 29936.37

Authors

Hung, L.-W.,Wang, I.X.,Nikaido, K.,Liu, P.-Q.,Ames, G.F.-L.,Kim, S.-H. (deposition date: 1998-11-12, release date: 1999-11-17, Last modification date: 2023-12-27)

Primary citation

Hung, L.W.,Wang, I.X.,Nikaido, K.,Liu, P.Q.,Ames, G.F.,Kim, S.H.
Crystal structure of the ATP-binding subunit of an ABC transporter.
Nature, 396:703-707, 1998

PubMed 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.

PubMed: 9872322
DOI: 10.1038/25393

Experimental method

X-RAY DIFFRACTION (1.5 Å)