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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1rbl

E.C. nameribulose-bisphosphate carboxylase
SpeciesSynechococcus sp. (Bacteria)
E.C. Number (IntEnz) 4.1.1.39
CSA Homologues of 1rblThere are 46 Homologs
CSA Entries With UniProtID P00880
CSA Entries With EC Number 4.1.1.39
PDBe Entry 1rbl
PDBSum Entry 1rbl
MACiE Entry 1rbl

Literature Report

IntroductionRibulose-1,5-bisphosphate carboxylase catalyses the only known mechanism whereby atmospheric carbon dioxide is fixed by living organisms. This enzyme is one of the most abundant on Earth, and of great economic importance. The enzyme has two types of subunit, the large are chloroplast encoded and the small subunit (of unknown function) is nuclear encoded. The active site contains a magnesium atom.
MechansimThis enzyme catalyses two opposing reaction, the first step in photosynthetic carbon dioxide fixation, the carboxylation of ribulose-1,5-bisphosphate (RuBP), and the first step in photorespiration, the oxygenation of RuBP. While the catalytic mechanism of the oxygenation is still not clear, the mechanism of the carboxylation of ribulose-1,5-bisphosphate (RuBP) is proposed as follows:
1) Proton abstraction of the substrate, RuBP. 2) Tautomerisation of the enediol to form a C2 carbanion. 3) Carboxylation by electrophilic attack of CO2 on the enediolate. 4) Hydration of the C3 ketone of the six-carbon intermediate. 5) Carbon-carbon cleavage initiated by deprotonation of the hydroxyl oxygen atoms at the C3 centre of the six-carbon intermediate. 6) Stereospecific protonation of the carbanion derived from C1 and C2 which produces the second molecule of D-3PGA.
Reaction

Catalytic Sites for 1rbl

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysA175172macie:sideChain
LysA201198macie:sideChain
LysA177174macie:sideChain
HisA294291macie:sideChain
AspA203200macie:sideChain
HisA327324macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysB175172macie:sideChain
LysB201198macie:sideChain
LysB177174macie:sideChain
HisB294291macie:sideChain
AspB203200macie:sideChain
HisB327324macie:sideChain

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysC175172macie:sideChain
LysC201198macie:sideChain
LysC177174macie:sideChain
HisC294291macie:sideChain
AspC203200macie:sideChain
HisC327324macie:sideChain

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysD175172macie:sideChain
LysD201198macie:sideChain
LysD177174macie:sideChain
HisD294291macie:sideChain
AspD203200macie:sideChain
HisD327324macie:sideChain

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysE175172macie:sideChain
LysE201198macie:sideChain
LysE177174macie:sideChain
HisE294291macie:sideChain
AspE203200macie:sideChain
HisE327324macie:sideChain

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysF175172macie:sideChain
LysF201198macie:sideChain
LysF177174macie:sideChain
HisF294291macie:sideChain
AspF203200macie:sideChain
HisF327324macie:sideChain

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysG175172macie:sideChain
LysG201198macie:sideChain
LysG177174macie:sideChain
HisG294291macie:sideChain
AspG203200macie:sideChain
HisG327324macie:sideChain

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
LysH175172macie:sideChain
LysH201198macie:sideChain
LysH177174macie:sideChain
HisH294291macie:sideChain
AspH203200macie:sideChain
HisH327324macie:sideChain

Literature References

Notes:
Newman J.
The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution
J Biol Chem 1993 268 25876-25886
PubMed: 8245022
Newman J.
Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate
Structure 1994 2 495-502
PubMed: 7922027
Andersson I.
Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate.
J Mol Biol 1996 259 160-174
PubMed: 8648644
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