5TWK
Crystal Structure of RlmH in Complex with Sinefungin
Summary for 5TWK
| Entry DOI | 10.2210/pdb5twk/pdb |
| Related | 5TWJ |
| Descriptor | Ribosomal RNA large subunit methyltransferase H, SINEFUNGIN (3 entities in total) |
| Functional Keywords | sinefungin, rna methyltransferase, spout, pseudouridine, helix 69, transferase, transferase-antibiotic complex, transferase/antibiotic |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 74697.99 |
| Authors | Koh, C.S.,Madireddy, R.,Beane, T.J.,Zamore, P.D.,Korostelev, A.A. (deposition date: 2016-11-14, release date: 2017-05-03, Last modification date: 2023-10-04) |
| Primary citation | Koh, C.S.,Madireddy, R.,Beane, T.J.,Zamore, P.D.,Korostelev, A.A. Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine. Sci Rep, 7:969-969, 2017 Cited by PubMed Abstract: Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Ψ1915), 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. PubMed: 28428565DOI: 10.1038/s41598-017-01186-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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