2.1.1.166: 23S rRNA (uridine2552-2'-O)-methyltransferase
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For detailed information about 23S rRNA (uridine2552-2'-O)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.166
Reaction
Synonyms
23 S ribosomal RNA methyltransferase, 23S rRNA methyltransferase, FTSJ, FtsJ/RrmJ heat shock protein, FtsJ2, heat shock protein RrmJ, Mj0697, RlmE, RrmJ, Um(2552) 23S ribosomal RNA methyltransferase, Um2552 methyltransferase
ECTree
2.1.1.166 23S rRNA (uridine2552-2'-O)-methyltransferaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 2.1.1.166 - 23S rRNA (uridine2552-2'-O)-methyltransferase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
crystal structure of the FtsJ protein at 1.5 A resolution in complex with its cofactor S-adenosyl-L-methionine
identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
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identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
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