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Literature summary for 2.1.1.178 extracted from

  • Hallberg, B.M.; Ericsson, U.B.; Johnson, K.A.; Andersen, N.M.; Douthwaite, S.; Nordlund, P.; Beuscher, A.E. 4th; Erlandsen, H.
    The structure of the RNA m5C methyltransferase YebU from Escherichia coli reveals a C-terminal RNA-recruiting PUA domain (2006), J. Mol. Biol., 360, 774-787.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the Escherichia coli YebU gene is cloned into the PT73.3HisGW vector.25 The resulting construct encodes a polypeptide with the YebU gene and both N- and C-terminal hexa-histidine tails Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
YebU crystals are grown at room temperature by the hanging-drop, vapour-diffusion method, Crystal structure solved at 2.9 A resolution. The enzyme has an N-terminal catalytic domain that binds S-adenosylmethionine. The C-terminal domain has structural similarity to PUA domains of pseudouridine synthases and archaeosine-specific transglycosylases. The YebU structure is used to propose the most likely mechanism for its substrate specificity and recognition Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P76273
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-

Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + cytosine1407 in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine1407 in 16S rRNA the YebU structure is used to propose the most likely mechanism for its substrate specificity and recognition Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + cytosine1407 in 16S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + 5-methylcytosine1407 in 16S rRNA
-
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Synonyms

Synonyms Comment Organism
RNA m5C methyltransferase YebU
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Escherichia coli
RsmF
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Escherichia coli
YebU
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Escherichia coli