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Literature summary for 2.1.1.271 extracted from

  • Schubert, H.L.; Wilson, K.S.; Raux, E.; Woodcock, S.C.; Warren, M.J.
    The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase (1998), Nat. Struct. Biol., 5, 585-592.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
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 Priestia megaterium
to 2.4 A resolution. The enzyme contains two alpha/beta domains forming a trough in which S-adenosyl-L-homocysteine binds. The entire structure follows a beta-alpha repeating pattern with the single exception of a beta-hairpin late in the C-terminal domain. A second crystal form determined at 3.1 A resolution highlights the flexibility of two loops around the S-adenosyl-L-homocysteine-binding site Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
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Priestia megaterium O87696
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Purification (Commentary)

Purification (Comment) Organism
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 Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + cobalt-precorrin-4
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 Priestia megaterium S-adenosyl-L-homocysteine + cobalt-precorrin-5
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