1E79

Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)

Summary for 1E79

• Entry DOI: 10.2210/pdb1e79/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1EFR 1NBM 1QO1
• Descriptor: ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, DICYCLOHEXYLUREA, SULFATE ION, ... (12 entities in total)
• Functional Keywords: atp phosphorylase, atp phosphorylase (h+ transporting), f1fo atp synthase, central stalk, hydrolase
• Biological source: BOS TAURUS (BOVINE); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631 P05630 P05632
• Total number of polymer chains: 9
• Total formula weight: 374930.30

Authors

Gibbons, C.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2000-08-25, release date: 2000-11-03, Last modification date: 2024-10-09)

Primary citation

Gibbons, C.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E.
The Structure of the Central Stalk in Bovine F(1)-ATPase at 2.4 A Resolution.
Nat.Struct.Biol., 7:1055-, 2000

PubMed Abstract: The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F(1)-ATPase, the protrusion was disordered, but with crystals of F(1)-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain.

PubMed: 11062563
DOI: 10.1038/80981

Experimental method

X-RAY DIFFRACTION (2.4 Å)