1MAB

RAT LIVER F1-ATPASE

Summary for 1MAB

• Entry DOI: 10.2210/pdb1mab/pdb
• Descriptor: PROTEIN (F1-ATPASE ALPHA CHAIN), PROTEIN (F1-ATPASE BETA CHAIN), PROTEIN (F1-ATPASE GAMMA CHAIN), ... (8 entities in total)
• Functional Keywords: atp synthase, fof1-atpase, oxidative phosphorylation, mitochondria, hydrolase
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Mitochondrion inner membrane : P15999; Mitochondrion: P10719 P35435
• Total number of polymer chains: 3
• Total formula weight: 137780.73

Authors

Bianchet, M.A.,Amzel, L.M. (deposition date: 1998-08-06, release date: 1998-09-30, Last modification date: 2024-05-22)

Primary citation

Bianchet, M.A.,Hullihen, J.,Pedersen, P.L.,Amzel, L.M.
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.
Proc.Natl.Acad.Sci.USA, 95:11065-11070, 1998

PubMed Abstract: During mitochondrial ATP synthesis, F1-ATPase-the portion of the ATP synthase that contains the catalytic and regulatory nucleotide binding sites-undergoes a series of concerted conformational changes that couple proton translocation to the synthesis of the high levels of ATP required for cellular function. In the structure of the rat liver F1-ATPase, determined to 2.8-A resolution in the presence of physiological concentrations of nucleotides, all three beta subunits contain bound nucleotide and adopt similar conformations. This structure provides the missing configuration of F1 necessary to define all intermediates in the reaction pathway. Incorporation of this structure suggests a mechanism of ATP synthesis/hydrolysis in which configurations of the enzyme with three bound nucleotides play an essential role.

PubMed: 9736690
DOI: 10.1073/pnas.95.19.11065

Experimental method

X-RAY DIFFRACTION (2.8 Å)