Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5IQ5

NMR solution structure of Mayaro virus macro domain

Summary for 5IQ5
Entry DOI10.2210/pdb5iq5/pdb
NMR InformationBMRB: 30043
DescriptorMacro domain (1 entity in total)
Functional Keywordsviral macro domains, mayaro virus, alphavirus, adp ribose binding module, viral protein
Biological sourceMayaro virus (strain Brazil) (MAYV)
Total number of polymer chains1
Total formula weight18147.49
Authors
Melekis, E.,Tsika, A.C.,Bentrop, D.,Papageorgiou, N.,Coutard, B.,Spyroulias, G.A. (deposition date: 2016-03-10, release date: 2017-12-20, Last modification date: 2024-06-19)
Primary citationTsika, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon