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Literature summary for 2.5.1.17 extracted from

  • Ortiz de Orue Lucana, D.; Hickey, N.; Hensel, M.; Klare, J.P.; Geremia, S.; Tiufiakova, T.; Torda, A.E.
    The crystal structure of the C-terminal domain of the Salmonella enterica PduO protein an old fold with a new heme-binding mode (2016), Front. Microbiol., 7, 1010 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Salmonella enterica

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method. The structure of PduOC co-crystallized with heme is solved (1.9 A resolution) showing an octameric assembly with four heme moieities Salmonella enterica

Organism

Organism UniProt Comment Textmining
Salmonella enterica A0A5Z8GIG6
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-

Purification (Commentary)

Purification (Comment) Organism
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 Salmonella enterica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in the active site, the corrin ring of Co(II)rrinoids is firmly locked in place by several amino acid side chains so as to facilitate the dissociation of the axial ligand Salmonella enterica ?
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-

Synonyms

Synonyms Comment Organism
ATP:Cob(I)alaminadenosyltransferase
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 Salmonella enterica
PduO protein
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 Salmonella enterica

Cofactor

Cofactor Comment Organism Structure
heme PduOC apoprotein shows strong heme binding. Octameric assembly with four heme moieities. The four heme groups are highly solvent-exposed and the heme iron is hexa-coordinated with bis-His ligation by histidines from different monomers. The absence of the C-terminal domain in PduO does not affect adenosyltransferase activity in vitro Salmonella enterica

General Information

General Information Comment Organism
metabolism the enzyme is involved in 1,2-propanediol utilization Salmonella enterica