5IQ5

NMR solution structure of Mayaro virus macro domain

5IQ5 の概要

• エントリーDOI: 10.2210/pdb5iq5/pdb
• NMR情報: BMRB: 30043
• 分子名称: Macro domain (1 entity in total)
• 機能のキーワード: viral macro domains, mayaro virus, alphavirus, adp ribose binding module, viral protein
• 由来する生物種: Mayaro virus (strain Brazil) (MAYV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18147.49

構造登録者

Melekis, E.,Tsika, A.C.,Bentrop, D.,Papageorgiou, N.,Coutard, B.,Spyroulias, G.A. (登録日: 2016-03-10, 公開日: 2017-12-20, 最終更新日: 2024-06-19)

主引用文献

Tsika, A.C.,Melekis, E.,Tsatsouli, S.A.,Papageorgiou, N.,Mate, M.J.,Canard, B.,Coutard, B.,Bentrop, D.,Spyroulias, G.A.
Deciphering the Nucleotide and RNA Binding Selectivity of the Mayaro Virus Macro Domain.
J.Mol.Biol., 431:2283-2297, 2019

PubMed Abstract: Mayaro virus (MAYV) is a member of Togaviridae family, which also includes Chikungunya virus as a notorious member. MAYV recently emerged in urban areas of the Americas, and this emergence emphasized the current paucity of knowledge about its replication cycle. The macro domain (MD) of MAYV belongs to the N-terminal region of its non-structural protein 3, part of the replication complex. Here, we report the first structural and dynamical characterization of a previously unexplored Alphavirus MD investigated through high-resolution NMR spectroscopy, along with data on its ligand selectivity and binding properties. The structural analysis of MAYV MD reveals a typical "macro" (ββαββαβαβα) fold for this polypeptide, while NMR-driven interaction studies provide in-depth insights into MAYV MD-ligand adducts. NMR data in concert with thermodynamics and biochemical studies provide convincing experimental evidence for preferential binding of adenosine diphosphate ribose (ADP-r) and adenine-rich RNAs to MAYV MD, thus shedding light on the structure-function relationship of a previously unexplored viral MD. The emerging differences with any other related MD are expected to enlighten distinct functions.

PubMed: 30998933
DOI: 10.1016/j.jmb.2019.04.013

実験手法

SOLUTION NMR