Cloned (Comment) | Organism |
---|---|
gene pduO, overexpression in Escherichia coli strain BL21 (DE3) and secretion to the medium | Bacillus cereus |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Bacillus cereus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | - |
gene pduO | - |
Purification (Comment) | Organism |
---|---|
recombinant PduO from Escherichia coli strain BL21 (DE3) cell culture medium | Bacillus cereus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
additional information | MgATP and Cob(II)alamin binding sites, structure comparison overview | Bacillus cereus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
PduO | - |
Bacillus cereus |
PduO-type ATP:cob(I)alamin adenosyltransferase | - |
Bacillus cereus |
General Information | Comment | Organism |
---|---|---|
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 |
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 |