Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites Implications for the Mechanism of Rotary Catalysis
@article{Menz2001StructureOB, title={Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites Implications for the Mechanism of Rotary Catalysis}, author={Robert Ian Menz and John E. Walker and Andrew G W Leslie}, journal={Cell}, year={2001}, volume={106}, pages={331-341} }
411 Citations
Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation
- Biology, ChemistryNature Structural &Molecular Biology
- 2011
The crystal structure of the ATP synthase catalytic complex (F1) from Escherichia coli described here reveals the structural basis for autoinhibition by one of its rotary stalk subunits, and adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme.
Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1–ATPase from bovine heart mitochondria
- Chemistry, BiologyProceedings of the National Academy of Sciences
- 2012
The molecular description of the mechanism of F1–ATPase is based mainly on high-resolution structures of the enzyme from mitochondria, coupled with direct observations of rotation in bacterial enzymes, and has captured another intermediate in the catalytic cycle, which helps to define the order of substrate release.
The structure of bovine F1‐ATPase inhibited by ADP and beryllium fluoride
- Chemistry, BiologyThe EMBO journal
- 2004
In the structure of F1‐ATPase with five bound ADP molecules (three in α‐subunits, one each in the βTP and βDP subunits), which has been determined, the conformation of αArg373 suggests that it senses the presence (or absence of the γ‐phosphate of ATP.
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase
- Chemistry, BiologyThe EMBO journal
- 2006
The shifts in position of the central stalk between two of the three copies of yeast F1 ATPase give new insight into the conformational changes that take place during rotational catalysis.
Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Å Resolution*
- Chemistry, BiologyJournal of Biological Chemistry
- 2007
The structure with bound azide represents the ADP inhibited state of the enzyme, and the new structure represents a ground state intermediate in the active catalytic cycle of ATP hydrolysis.
A bi-site mechanism for Escherichia coli F1-ATPase accounts for the observed positive catalytic cooperativity.
- Biology, ChemistryBiochimica et biophysica acta
- 2009
How azide inhibits ATP hydrolysis by the F-ATPases.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 2006
The structure of bovine F1-ATPase determined at 1.95-A resolution with crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate, and azide explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding ofADP.
Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites.
- Chemistry, BiologyProceedings of the National Academy of Sciences of the United States of America
- 2005
It is concluded that ATP binding to a second catalytic site is sufficient to support rapid rates of catalysis.
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1
- Biology, ChemistryOpen Biology
- 2013
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF1 has been determined and provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule.
Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)
- Biology, Chemistry
- 2003
The energetics associated with two different models of the reaction steps, analysed using molecular dynamics calculations, show that three-nucleotide intermediates do not occur in configurations with an open β subunit; instead, they are stabilized by completing a jaw-like motion that closes the β sub unit around the nucleotide.
References
SHOWING 1-10 OF 84 REFERENCES
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
- ChemistryNature
- 1994
The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
- ChemistryNature Structural Biology
- 2000
The central stalk in ATP synthase is made of γ, δ and ɛ subunits in the mitochondrial enzyme, and with crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed.
Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride.
- Chemistry, BiologyStructure
- 2000
The ATP synthase--a splendid molecular machine.
- ChemistryAnnual review of biochemistry
- 1997
An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanism…
ATP Synthesis by Rotary Catalysis (Nobel lecture).
- ChemistryAngewandte Chemie
- 1998
The cyclic modulation of nucleotide-binding properties of the three catalytic β subunits by a series of conformational changes was an attractive explanation for the postulated binding change…
Structure of the gamma-epsilon complex of ATP synthase.
- ChemistryNature structural biology
- 2000
The crystal structure of a complex of the epsilon-sub unit and the central domain of the gamma-subunit refined at 2.1 A resolution reveals how rotation of these subunits causes large conformational changes in F(1), and thereby provides new insights into energy coupling between F(o) and F( 1).
Rotation of subunits during catalysis by Escherichia coli F1-ATPase.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1995
The results demonstrate that gamma subunit rotates relative to the beta subunits during catalysis, and similar reactivities of unlabeled and radiolabeled beta sub units with gamma C87 upon reoxidation.
Crystallization of F1-ATPase from bovine heart mitochondria.
- ChemistryJournal of molecular biology
- 1993
Crystals of the F1-ATPase sector of the ATP synthase complex from bovine heart mitochondria have been grown from solutions containing polyethylene glycol 6000. The crystals diffract to 2.9 A…
Molecular architecture of the rotary motor in ATP synthase.
- ChemistryScience
- 1999
An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits whose extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.