Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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Methanothermobacter thermautotrophicus | O26249 | - |
- |