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Catalytic Site Atlas Search Results
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Catalytic Site Atlas

CSA LITERATURE entry for 1g24

E.C. nameEXOENZYME C3
SpeciesClostridium botulinum (strain ATCC 19397 / Type A)
E.C. Number (IntEnz) 2.4.2.-
CSA Homologues of 1g24There are 40 Homologs
CSA Entries With UniProtID
CSA Entries With EC Number 2.4.2.-
PDBe Entry 1g24
PDBSum Entry 1g24
MACiE Entry 1g24

Literature Report

IntroductionClostridium boltulinum C3 exoenzyme catalyses the transfer of the ADP-ribose moiety of NAD onto asparagine 41 of the small GTP-binding protein Rho. This ADP-ribosylation inactivates Rho, blocking Rho activity in regulating the cytoskeleton and leading to cytoskeleton depolymerisation.
MechansimThe reaction requires loss of the nicotinamide moiety of NAD and attack on the C1' of ribose by Asn 41 of Rho. The oxocarbenium-like transition state is thought to be stabilised by Glu 214, which forms a hydrogen bond to the ribose 2' OH group. This interaction would increase electron density near C1' in the transition state.

Catalytic Sites for 1g24

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA214214macie:sideChainStabilises positive charge in the oxocarbenium-like transition state by forming a hydrogen bond to the 2' OH group of the ribose moiety.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB1214214macie:sideChainStabilises positive charge in the oxocarbenium-like transition state by forming a hydrogen bond to the 2' OH group of the ribose moiety.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluC2214214macie:sideChainStabilises positive charge in the oxocarbenium-like transition state by forming a hydrogen bond to the 2' OH group of the ribose moiety.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluD3214214macie:sideChainStabilises positive charge in the oxocarbenium-like transition state by forming a hydrogen bond to the 2' OH group of the ribose moiety.

Literature References

Notes:
Han S
Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis.
J Mol Biol 2001 305 95-107
PubMed: 11114250
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