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Catalytic Site Atlas Version 2.2.12
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CSA entry for 1ohh
Original Entry
Title:
Synthase
Compound:
Atp synthase alpha chain heart isoform, mitochondrial
Mutant:
No
UniProt/Swiss-Prot:
P00829-ATP0_BOVIN
P19483-ATPB_BOVIN
EC Class:
3.6.1.34
Other CSA Entries:
Overview of all sites for 1ohh
Homologues of 1ohh
Entries for UniProt/Swiss-Prot: P00829
Entries for UniProt/Swiss-Prot: P19483
Entries for EC: 3.6.1.34
Other Databases:
PDB entry: 1ohh
PDBsum entry: 1ohh
UniProt/Swiss-Prot: P00829
UniProt/Swiss-Prot: P19483
IntEnz entry: 3.6.1.34
Literature Report:
Introduction:
ATP synthase/F1F0-ATPase utilises the proton motive force generated by photosynthesis and oxidative phosphorylation to synthesise ATP. It also catalyses the hydrolysis of ATP. It is composed of 2 major domains, a catalytic F1 domain and a F0 proton-translocating domain, linked by a central stalk.
Mechanism:
The most widely accepted mechanism of ATP synthase is the binding change mechanism. The mechanism suggests that the three catalytic sites of ATP synthase have different nucleotide binding affinities, of which one has very low substrate binding affinity, one can bind substrates reversibly and one has a very high affinity such that ATP can form spontaneously from ADP and Pi. The rotation of the central stalk, driven by the proton motive force, changes the conformation of the beta-subunits and thus the binding affinity of the 3 catalytic sites, taking each through cycles of the 3 affinity states and hence catalysing the synthesis and hydrolysis of ATP. Though, it is worthwhile to note that there are still disagreements on some of the proposals in the mechanism.

The transition state of the phosphoryl transfer is general accepted as a pentacovalent phosphorus with 2 apical and 3 equatorial bonds. This transition state of the phosphoryl transfer is stabilised by 3 residues, alpha-Arg373, beta-Lys162 and beta-Arg189. In hydrolysis of ATP, beta-Glu188 polarises and activates a deprotonated water molecule for an inline nucleophilic attack on the terminal-phosphate of the ATP.
Sites:

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ARGA 373 416Sidechain
ElectrostaticTransition state
It stabilises the pentacovalent negatively charged phosphorus transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 11509182 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 10569931 Current protein Mutagenesis of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
LYSE 162 212Sidechain
ElectrostaticTransition state
It stabilises the pentacovalent negatively charged phosphorus transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 11509182 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 9013618 Current protein Mutagenesis of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
GLUE 188 238Sidechain
Acid/baseWater
It acts as a base to deprotonate, thus activating a water molecule to allow its nucleophilic attack on the terminal phosphate of ATP in hydrolysis of ATP.
Evidence from paper Evidence concerns Evidence type
PubMed ID 11509182 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 9013618 Current protein Mutagenesis of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ARGE 189 239Sidechain
ElectrostaticTransition state
It stabilises the pentacovalent negatively charged phosphorus transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10387006 Current protein Mutagenesis of residue
PubMed ID 11509182 Current protein Residue is positioned appropriately (ligand position known)
References:
1
Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization.
S. Nadanaciva and J. Weber and S. Wilke-Mounts and A. E. Senior
Biochemistry 38, (47) 15493-9, (1999).
10569931
2
Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
R. I. Menz and J. E. Walker and A. G. Leslie
Cell 106, (3) 331-41, (2001).
11509182
3
The role of beta-Arg-182, an essential catalytic site residue in Escherichia coli F1-ATPase.
S. Nadanaciva and J. Weber and A. E. Senior
Biochemistry 38, (24) 7670-7, (1999).
10387006
4
F1-ATPase, roles of three catalytic site residues.
S. Löbau and J. Weber and S. Wilke-Mounts and A. E. Senior
J Biol Chem 272, (6) 3648-56, (1997).
9013618
5
The molecular mechanism of ATP synthesis by F1F0-ATP synthase.
A. E. Senior and S. Nadanaciva and J. Weber
Biochim Biophys Acta 1553, (3) 188-211, (2002).
11997128
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