5IQ5
NMR solution structure of Mayaro virus macro domain
Summary for 5IQ5
| Entry DOI | 10.2210/pdb5iq5/pdb |
| NMR Information | BMRB: 30043 |
| Descriptor | Macro domain (1 entity in total) |
| Functional Keywords | viral macro domains, mayaro virus, alphavirus, adp ribose binding module, viral protein |
| Biological source | Mayaro virus (strain Brazil) (MAYV) |
| Total number of polymer chains | 1 |
| Total formula weight | 18147.49 |
| 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 citation | 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 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: 30998933DOI: 10.1016/j.jmb.2019.04.013 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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