7MJW

Methylated MiaB in the complex with 5'-deoxyadenosine, methionine and RNA

7MJW の概要

• エントリーDOI: 10.2210/pdb7mjw/pdb
• 分子名称: tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase, RNA (5'-R(*GP*GP*AP*CP*UP*GP*AP*AP*(MIA)P*AP*UP*CP*C)-3'), FE3-S4 methylated cluster, ... (8 entities in total)
• 機能のキーワード: trna-2-methylthio-n(6)-dimethylallyladenosine synthase, transferase, transferase-rna complex, transferase/rna
• 由来する生物種: Bacteroides uniformis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 113214.74

構造登録者

Esakova, O.A.,Grove, T.L.,Yennawar, N.H.,Arcinas, A.J.,Wang, B.,Krebs, C.,Almo, S.C.,Booker, S.J. (登録日: 2021-04-20, 公開日: 2021-09-15, 最終更新日: 2023-10-18)

主引用文献

Esakova, O.A.,Grove, T.L.,Yennawar, N.H.,Arcinas, A.J.,Wang, B.,Krebs, C.,Almo, S.C.,Booker, S.J.
Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB.
Nature, 597:566-570, 2021

PubMed Abstract: Numerous post-transcriptional modifications of transfer RNAs have vital roles in translation. The 2-methylthio-N-isopentenyladenosine (msiA) modification occurs at position 37 (A37) in transfer RNAs that contain adenine in position 36 of the anticodon, and serves to promote efficient A:U codon-anticodon base-pairing and to prevent unintended base pairing by near cognates, thus enhancing translational fidelity. The msiA modification is installed onto isopentenyladenosine (iA) by MiaB, a radical S-adenosylmethionine (SAM) methylthiotransferase. As a radical SAM protein, MiaB contains one [FeS] cluster used in the reductive cleavage of SAM to form a 5'-deoxyadenosyl 5'-radical, which is responsible for removing the C hydrogen of the substrate. MiaB also contains an auxiliary [FeS] cluster, which has been implicated in sulfur transfer to C of iA37. How this transfer takes place is largely unknown. Here we present several structures of MiaB from Bacteroides uniformis. These structures are consistent with a two-step mechanism, in which one molecule of SAM is first used to methylate a bridging µ-sulfido ion of the auxiliary cluster. In the second step, a second SAM molecule is cleaved to a 5'-deoxyadenosyl 5'-radical, which abstracts the C hydrogen of the substrate but only after C has undergone rehybridization from sp to sp. This work advances our understanding of how enzymes functionalize inert C-H bonds with sulfur.

PubMed: 34526715
DOI: 10.1038/s41586-021-03904-6

実験手法

X-RAY DIFFRACTION (1.4 Å)