spacer
View the latest EBI news stories and important announcements...
more

spacer
Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1ohh

E.C. nameH+-transporting two-sector ATPase
SpeciesBos taurus (Bovine)
E.C. Number (IntEnz) 3.6.3.14
CSA Homologues of 1ohhThere are 58 Homologs
CSA Entries With UniProtID P00829
CSA Entries With EC Number 3.6.3.14
PDBe Entry 1ohh
PDBSum Entry 1ohh
MACiE Entry M0178

Literature Report

IntroductionATP 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.
MechansimThe 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.
Reaction

Catalytic Sites for 1ohh

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgD356406macie:sideChainError

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgE356406macie:sideChainError

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgF356406macie:sideChainError

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgA373416macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.
ArgE189239macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.
GluE188238macie:sideChainIt 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.
LysE162212macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgC373416macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.
ArgD189239macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.
GluD188238macie:sideChainIt 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.
LysD162212macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgF189239macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.
GluF188238macie:sideChainIt 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.
LysF162212macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.
ArgB373416macie:sideChainIt stabilises the pentacovalent negatively charged phosphorus transition state.

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysA175218macie:sideChainError
LysA209252macie:sideChainError
GlnA208251macie:sideChainError

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysB175218macie:sideChainError
LysB209252macie:sideChainError
GlnB208251macie:sideChainError

Annotated By Reference To The Literature - Site 9 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysC175218macie:sideChainError
LysC209252macie:sideChainError
GlnC208251macie:sideChainError

Literature References

Notes:
Nadanaciva S
Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization.
Biochemistry 1999 38 15493-15499
PubMed: 10569931
Menz RI
Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
Cell 2001 106 331-341
PubMed: 11509182
Nadanaciva S
The role of beta-Arg-182, an essential catalytic site residue in Escherichia coli F1-ATPase.
Biochemistry 1999 38 7670-7677
PubMed: 10387006
Löbau S
F1-ATPase, roles of three catalytic site residues.
J Biol Chem 1997 272 3648-3656
PubMed: 9013618
Senior AE
The molecular mechanism of ATP synthesis by F1F0-ATP synthase.
Biochim Biophys Acta 2002 1553 188-211
PubMed: 11997128
spacer
spacer