2yxl | pdb_00002yxl

Crystal Structure of PH0851

spinqualitylabelsall models 2yxl, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yxl is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SFG Gene: PH0851 (Pyrococcus horikoshii) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed One of the modified nucleosides that frequently occurs in rRNAs and tRNAs is 5-methylcytidine (m(5)C). Escherichia coli Fmu/RsmB/RrmB is an S-adenosyl-L-methionine (AdoMet)-dependent methyltransferase that forms m(5)C967 in 16S rRNA. Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m(5)C methyltransferase family. In the present study, the crystal structure of a homologue of E. coli Fmu/RsmB/RrmB from the archaeon Pyrococcus horikoshii (PH0851) complexed with an AdoMet analogue was determined at 2.55 A resolution. The structure and sequence of the C-terminal catalytic domain are highly conserved compared with those of E. coli Fmu/RsmB/RrmB. In contrast, the sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies. Nevertheless, the N-terminal domains of PH0851 and E. coli Fmu/RsmB/RrmB are both alpha-helical and adopt a similar topology. Next to the AdoMet-binding site, a positively charged cleft is formed between the N- and C-terminal domains. This cleft is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate. Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase.,Hikida Y, Kuratani M, Bessho Y, Sekine SI, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1301-7. Epub 2010, Nov 16. PMID:21123870 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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