Literature summary extracted from
Park, A.K.; Chi, Y.M.; Moon, J.H.
Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP (2011), Biochem. Biophys. Res. Commun., 408, 417-421.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.5.1.17 |
gene pduO, overexpression in Escherichia coli strain BL21 (DE3) and secretion to the medium |
Bacillus cereus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.5.1.17 |
purified recombinant PduO in complex with ATP, hanging drop vapor diffusion method, mixing o 0.001 ml of 13 mg/ml protein solution, with or without 4 mM ATP and 4 mM MgCl2, with 0.001 ml of optimized reservoir solution containing 100 mM MES, pH 6.5, 1.52 M ammonium sulfate, 9% v/v dioxane, followed by equilibration over 0.5 ml of the mother liquor, the cryoprotection solution contains 50 mM MES, pH 6.5, 0.76 M ammonium sulfate, 4.5% v/v dioxane, and 1.7 M sodium malonate, pH 7.0, X-ray diffraction structure determination and analysis |
Bacillus cereus |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.5.1.17 |
Mg2+ |
required |
Bacillus cereus |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.5.1.17 |
additional information |
Bacillus cereus |
ATP:Cobalamin adenosyltransferases catalyze the transfer a 5'-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12 |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.5.1.17 |
Bacillus cereus |
- |
gene pduO |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.5.1.17 |
recombinant PduO from Escherichia coli strain BL21 (DE3) cell culture medium |
Bacillus cereus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.5.1.17 |
additional information |
ATP:Cobalamin adenosyltransferases catalyze the transfer a 5'-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12 |
Bacillus cereus |
? |
- |
? |
|
2.5.1.17 |
additional information |
MgATP and Cob(II)alamin binding sites, structure comparison overview |
Bacillus cereus |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.5.1.17 |
More |
structural comparisons between apo BcPduO and BcPduO in complex with MgATP reveal that the N-terminal strands of both structures are ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Apo BcPduO is bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site |
Bacillus cereus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.5.1.17 |
PduO |
- |
Bacillus cereus |
2.5.1.17 |
PduO-type ATP:cob(I)alamin adenosyltransferase |
- |
Bacillus cereus |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.5.1.17 |
evolution |
cob(I)alamin adenosyltransferases are separated into three type groups according to their amino acid sequences: CobA, PduO, and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases are the most widely distributed enzyme type. Whereas the CobA-type enzyme, which is constitutively expressed, is encoded by the cobA gene, PduO and EutT-type adenosyltransferases are encoded within large operons whose functions are required for the catabolism of 1,2-propanediol or ethanolamine. Despite the fact that all three families of adenosyltransferases catalyze the same overall reaction, they share little sequence identity of below 20% and the CobA and PduO enzymes have fairly different three-dimensional structures |
Bacillus cereus |
2.5.1.17 |
additional information |
structural comparisons between apo BcPduO and BcPduO in complex with MgATP reveal that the N-terminal strands of both structures are ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Apo BcPduO is bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site |
Bacillus cereus |