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Literature summary for 2.1.1.196 extracted from

  • Keller, J.P.; Smith, P.M.; Benach, J.; Christendat, D.; de Titta, G.T.; Hunt, J.F.
    The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase (2002), Structure, 10, 1475-1487.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
homotetrameric apo form of CbiT crystallized in several space groups, to about 2.5 A resolution, and in complex with S-adenosyl-L-homocysteine, to 1.9 A resolution. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and the cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that can accommodate a precorrin substrate. CbiT probably functions as a precorrin methyltransferase Methanothermobacter thermautotrophicus

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus O26249
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