3ZIA

The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1

Summary for 3ZIA

• Entry DOI: 10.2210/pdb3zia/pdb
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, 1,2-ETHANEDIOL, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ... (11 entities in total)
• Functional Keywords: hydrolase, natural inhibitor, catalysis, intermediate
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 20
• Total formula weight: 761396.94

Authors

Robinson, G.C.,Bason, J.V.,Montgomery, M.G.,Fearnley, I.M.,Mueller, D.M.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2013-01-07, release date: 2013-02-13, Last modification date: 2023-12-20)

Primary citation

Robinson, G.C.,Bason, J.V.,Montgomery, M.G.,Fearnley, I.M.,Mueller, D.M.,Leslie, A.G.W.,Walker, J.E.
The Structure of F1-ATPase from Saccharomyces Cerevisiae Inhibited by its Regulatory Protein If1.
Open Biol., 3:164-, 2013

PubMed Abstract: The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF₁ has been determined at 2.5 Å resolution. The inhibitory region of IF₁ from residues 1 to 36 is entrapped between the C-terminal domains of the α(DP)- and β(DP)-subunits in one of the three catalytic interfaces of the enzyme. Although the structure of the inhibited complex is similar to that of the bovine-inhibited complex, there are significant differences between the structures of the inhibitors and their detailed interactions with F₁-ATPase. However, the most significant difference is in the nucleotide occupancy of the catalytic β(E)-subunits. The nucleotide binding site in β(E)-subunit in the yeast complex contains an ADP molecule without an accompanying magnesium ion, whereas it is unoccupied in the bovine complex. Thus, the structure provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule.

PubMed: 23407639
DOI: 10.1098/RSOB.120164

Experimental method

X-RAY DIFFRACTION (2.5 Å)