6UET
SAM-bound SAM-IV riboswitch
Summary for 6UET
Entry DOI | 10.2210/pdb6uet/pdb |
EMDB information | 20755 20756 |
Descriptor | RNA (119-MER), S-ADENOSYLMETHIONINE (2 entities in total) |
Functional Keywords | sam-iv riboswitch, cryo-em, small rna, rna |
Biological source | Mycobacterium sp. MCS |
Total number of polymer chains | 1 |
Total formula weight | 38921.34 |
Authors | Zhang, K.,Li, S.,Kappel, K.,Pintilie, G.,Su, Z.,Mou, T.,Schmid, M.,Das, R.,Chiu, W. (deposition date: 2019-09-23, release date: 2019-12-18, Last modification date: 2024-03-20) |
Primary citation | Zhang, K.,Li, S.,Kappel, K.,Pintilie, G.,Su, Z.,Mou, T.C.,Schmid, M.F.,Das, R.,Chiu, W. Cryo-EM structure of a 40 kDa SAM-IV riboswitch RNA at 3.7 angstrom resolution. Nat Commun, 10:5511-5511, 2019 Cited by PubMed Abstract: Specimens below 50 kDa have generally been considered too small to be analyzed by single-particle cryo-electron microscopy (cryo-EM). The high flexibility of pure RNAs makes it difficult to obtain high-resolution structures by cryo-EM. In bacteria, riboswitches regulate sulfur metabolism through binding to the S-adenosylmethionine (SAM) ligand and offer compelling targets for new antibiotics. SAM-I, SAM-I/IV, and SAM-IV are the three most commonly found SAM riboswitches, but the structure of SAM-IV is still unknown. Here, we report the structures of apo and SAM-bound SAM-IV riboswitches (119-nt, ~40 kDa) to 3.7 Å and 4.1 Å resolution, respectively, using cryo-EM. The structures illustrate homologies in the ligand-binding core but distinct peripheral tertiary contacts in SAM-IV compared to SAM-I and SAM-I/IV. Our results demonstrate the feasibility of resolving small RNAs with enough detail to enable detection of their ligand-binding pockets and suggest that cryo-EM could play a role in structure-assisted drug design for RNA. PubMed: 31796736DOI: 10.1038/s41467-019-13494-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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