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 1j70

E.C. namesulfate adenylyltransferase
SpeciesSaccharomyces cerevisiae (Baker's yeast)
E.C. Number (IntEnz) 2.7.7.4
CSA Homologues of 1j70There are 17 Homologs
CSA Entries With UniProtID P08536
CSA Entries With EC Number 2.7.7.4
PDBe Entry 1j70
PDBSum Entry 1j70
MACiE Entry M0287

Literature Report

IntroductionATP sulphurylases catalyse the reaction of inorganic sulfate with ATP to form adenosine-5'-phosphosulfate and pyrophosphate in the primary step of intracellular sulfate activation.
ATP sulphurylase is classified into the superfamily of alpha/beta phosphodiesterases.
MechansimATP sulphurylase catalyses the reaction mostly by simply bringing the substrate in a close proximity and appropriate conformation. ATP is able to make an in-line nucleophilic attack on the adjacent sulfate with stereochemical inversion at the alpha-phosphorous leading directly to the formation of APS with pyrophosphate as a leaving group. The enzyme is able to donate a proton through Arg 197 to facilitate cleavage. The pentavalent transition state is stabilised using His 201 and His 204 side-chains.
Reaction

Catalytic Sites for 1j70

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA204204macie:sideChainStabilises the pentacoordinate transition state.
HisA201201macie:sideChainStabilises the pentacoordinate transition state.
ArgA197197macie:sideChainActs as a proton donor to facilitate collapse of the intermediate.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisB204204macie:sideChainStabilises the pentacoordinate transition state.
HisB201201macie:sideChainStabilises the pentacoordinate transition state.
ArgB197197macie:sideChainActs as a proton donor to facilitate collapse of the intermediate.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisC204204macie:sideChainStabilises the pentacoordinate transition state.
HisC201201macie:sideChainStabilises the pentacoordinate transition state.
ArgC197197macie:sideChainActs as a proton donor to facilitate collapse of the intermediate.

Literature References

Notes:
Beynon JD
Crystal structure of ATP sulfurylase from the bacterial symbiont of the hydrothermal vent tubeworm Riftia pachyptila.
Biochemistry 2001 40 14509-14517
PubMed: 11724564
Rajeev Motwani
The Probabilistic Method Yields Deterministic Parallel Algorithms
J Biol Chem 1979 254 3537-3542
PubMed: 107174
Deyrup AT
Chemical modification and site-directed mutagenesis of conserved HXXH and PP-loop motif arginines and histidines in the murine bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase.
J Biol Chem 1999 274 28929-28936
PubMed: 10506138
Ullrich TC
Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation.
EMBO J 2001 20 316-329
PubMed: 11157739
Lalor DJ
Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity.
Protein Eng 2003 16 1071-1079
PubMed: 14983089
Venkatachalam KV
Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase.
J Biol Chem 1999 274 2601-2604
PubMed: 9915785
spacer
spacer