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.
Wurm
Jan Philip
JP
Institut für Molekulare Biowissenschaften, Johann-Wolfgang-Goethe-Universität Frankfurt/M., Frankfurt, Germany.
Duchardt
Elke
E
Meyer
Britta
B
Leal
Belinda Z
BZ
Kötter
Peter
P
Entian
Karl-Dieter
KD
Wöhnert
Jens
J
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