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Literature summary for 2.5.1.17 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene pduO, overexpression in Escherichia coli strain BL21 (DE3) and secretion to the medium Bacillus cereus

Crystallization (Commentary)

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

Metals/Ions Comment Organism Structure
Mg2+ required Bacillus cereus

Natural Substrates/ Products (Substrates)

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 ?
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?

Organism

Organism UniProt Comment Textmining
Bacillus cereus
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gene pduO
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Purification (Commentary)

Purification (Comment) Organism
recombinant PduO from Escherichia coli strain BL21 (DE3) cell culture medium Bacillus cereus

Substrates and Products (Substrate)

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 ?
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?

Subunits

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

Synonyms Comment Organism
PduO
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Bacillus cereus
PduO-type ATP:cob(I)alamin adenosyltransferase
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Bacillus cereus

General Information

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