4X62

Crystal Structure of 30S ribosomal subunit from Thermus thermophilus

Summary for 4X62

• Entry DOI: 10.2210/pdb4x62/pdb
• Descriptor: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (28 entities in total)
• Functional Keywords: 30s ribosomal subunit m6a decoding mrna modification, ribosome-antibiotic complex, ribosome/antibiotic
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 23
• Total formula weight: 784709.84

Authors

Demirci, H.,Chen, J.,Choi, J.,Soltis, M.,Puglisi, J.D. (deposition date: 2014-12-06, release date: 2015-11-18, Last modification date: 2019-12-25)

Primary citation

Choi, J.,Ieong, K.W.,Demirci, H.,Chen, J.,Petrov, A.,Prabhakar, A.,O'Leary, S.E.,Dominissini, D.,Rechavi, G.,Soltis, S.M.,Ehrenberg, M.,Puglisi, J.D.
N(6)-methyladenosine in mRNA disrupts tRNA selection and translation-elongation dynamics.
Nat.Struct.Mol.Biol., 23:110-115, 2016

PubMed Abstract: N(6)-methylation of adenosine (forming m(6)A) is the most abundant post-transcriptional modification within the coding region of mRNA, but its role during translation remains unknown. Here, we used bulk kinetic and single-molecule methods to probe the effect of m(6)A in mRNA decoding. Although m(6)A base-pairs with uridine during decoding, as shown by X-ray crystallographic analyses of Thermus thermophilus ribosomal complexes, our measurements in an Escherichia coli translation system revealed that m(6)A modification of mRNA acts as a barrier to tRNA accommodation and translation elongation. The interaction between an m(6)A-modified codon and cognate tRNA echoes the interaction between a near-cognate codon and tRNA, because delay in tRNA accommodation depends on the position and context of m(6)A within codons and on the accuracy level of translation. Overall, our results demonstrate that chemical modification of mRNA can change translational dynamics.

PubMed: 26751643
DOI: 10.1038/nsmb.3148

Experimental method

X-RAY DIFFRACTION (3.4492 Å)