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3E5F

Crystal Structures of the SMK box (SAM-III) Riboswitch with Se-SAM

Summary for 3E5F
Entry DOI10.2210/pdb3e5f/pdb
Related3e5C 3e5e
DescriptorSMK box (SAM-III) Riboswitch for RNA, STRONTIUM ION, [(3S)-3-amino-4-hydroxy-4-oxo-butyl]-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl]-methyl-selanium, ... (4 entities in total)
Functional Keywordssmk sam riboswitch shine-delgarno translation regulation, rna
Total number of polymer chains1
Total formula weight19162.96
Authors
Lu, C. (deposition date: 2008-08-13, release date: 2008-10-07, Last modification date: 2024-02-21)
Primary citationLu, C.,Smith, A.M.,Fuchs, R.T.,Ding, F.,Rajashankar, K.,Henkin, T.M.,Ke, A.
Crystal structures of the SAM-III/S(MK) riboswitch reveal the SAM-dependent translation inhibition mechanism.
Nat.Struct.Mol.Biol., 15:1076-1083, 2008
Cited by
PubMed Abstract: Three distinct classes of S-adenosyl-L-methionine (SAM)-responsive riboswitches have been identified that regulate bacterial gene expression at the levels of transcription attenuation or translation inhibition. The S(MK) box (SAM-III) translational riboswitch has been identified in the SAM synthetase gene in members of the Lactobacillales. Here we report the 2.2-A crystal structure of the Enterococcus faecalis S(MK) box riboswitch. The Y-shaped riboswitch organizes its conserved nucleotides around a three-way junction for SAM recognition. The Shine-Dalgarno sequence, which is sequestered by base-pairing with the anti-Shine-Dalgarno sequence in response to SAM binding, also directly participates in SAM recognition. The riboswitch makes extensive interactions with the adenosine and sulfonium moieties of SAM but does not appear to recognize the tail of the methionine moiety. We captured a structural snapshot of the S(MK) box riboswitch sampling the near-cognate ligand S-adenosyl-L-homocysteine (SAH) in which SAH was found to adopt an alternative conformation and fails to make several key interactions.
PubMed: 18806797
DOI: 10.1038/nsmb.1494
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

231029

數據於2025-02-05公開中

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