5twk | pdb_00005twk

Crystal Structure of RlmH in Complex with Sinefungin

spinqualitylabelsall models 5twk, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5twk is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SFG Related: 5twj Activity: 23S rRNA (pseudouridine(1915)-N(3))-methyltransferase, with EC number 2.1.1.177 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RLMH_ECO45] Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Publication Abstract from PubMed Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Psi1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture. Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.,Koh CS, Madireddy R, Beane TJ, Zamore PD, Korostelev AA Sci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. PMID:28428565 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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