Backbone resonance assignments of the 48 kDa dimeric putative  18S rRNA-methyltransferase Nep1 from Methanocaldococcus  jannaschii.
Nep1 from Methanocaldococcus jannaschii is a 48 kDa dimeric protein belonging to the SPOUT-class of S-adenosylmethionine dependent RNA-methyltransferases and acting as a ribosome assembly factor. Mutations in the human homolog are the cause of Bowen-Conradi syndrome. We report here 1H, 15N and 13C chemical shift assignments for the backbone of the protein in its apo state.
Institut für Molekulare Biowissenschaften, Johann-Wolfgang-Goethe-Universität Frankfurt/M., Frankfurt, Germany.
Jan Philip
JP
Wurm
Elke
E
Duchardt
Britta
B
Meyer
Belinda Z
BZ
Leal
Peter
P
Kötter
Karl-Dieter
KD
Entian
Jens
J
Wöhnert
D017015:Methanococcales / Q000201:enzymology*; D008780:Methyltransferases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012337:RNA, Ribosomal, 18S / Q000378:metabolism*
D012337:RNA, Ribosomal, 18S; D008780:Methyltransferases