3nk7

Structure of the Nosiheptide-resistance methyltransferase S-adenosyl-L-methionine Complex

spinqualitylabelsall models 3nk7, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nk7 is a 2 chain structure with sequence from Streptomyces actuosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NSHR_STRAS Specifically methylates the adenosine-1067 in 23S ribosomal RNA. Confers resistance to antibiotic nosiheptide. 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 Nosiheptide-resistance methyltransferase (NHR) of Streptomyces actuosus is a class IV methyltransferase of the SpoU family and methylates 23S rRNA at nucleotide Adenosine corresponding to A1067 in Escherichia Coli. Such methylation is essential for resistance against nosiheptide, a sulphur peptide antibiotic, which is produced by the nosiheptide -producing strain, Streptomyces actuosus. Here, we report the crystal structures of NHR and NHR in complex with SAM (S-adenosyl-L-methionine) at 2.0 and 2.1 A resolution, respectively. NHR forms a functional homodimer and dimerization is required for methyltransferase activity. The monomeric NHR is comprised of N-terminal RNA binding domain (NTD) and C-terminal catalytic domain (CTD). Overall, the structure of NHR suggests that the methyltransferase activity is achieved by "reading" the RNA substrate with NTD and "adding" methyl group using CTD. Comprehensive mutagenesis and methyltransferase activity assays reveal critical regions for SAM binding in CTD and loops (L1 and L3) essential for RNA recognition in NTD. Finally, the catalytic mechanism and structural model that NHR recognize 23S rRNA is proposed based on the structural and biochemical analyses. Thus, our systematic structural studies reveal the substrate recognition and modification by the nosiheptide-resistance methyltransferase. Crystal Structure of the Nosiheptide Resistance Methyltransferase of Streptomyces actuosus.,Yang H, Wang Z, Shen Y, Wang P, Jia X, Zhao L, Zhou P, Gong R, Li Z, Yang Y, Chen D, Murchie A, Xu Y Biochemistry. 2010 Jun 15. PMID:20550164 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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