5MQX
NMR solution structure of macro domain from Venezuelan equine encephalitis virus(VEEV) in complex with ADP-ribose
Summary for 5MQX
| Entry DOI | 10.2210/pdb5mqx/pdb |
| NMR Information | BMRB: 26753 |
| Descriptor | Non-structural protein3, ADENOSINE-5-DIPHOSPHORIBOSE (2 entities in total) |
| Functional Keywords | macro domain, venezuelan equine encephalitis virus, alphavirus, adp-ribose, viral protein, non-structural protein 3 |
| Biological source | Venezuelan equine encephalitis virus (strain P676) (VEEV) |
| Total number of polymer chains | 1 |
| Total formula weight | 18663.81 |
| Authors | Makrynitsa, G.I.,Ntonti, D.,Marousis, K.D.,Matsoukas, M.T.,Papageorgiou, N.,Coutard, B.,Bentrop, D.,Spyroulias, G.A. (deposition date: 2016-12-21, release date: 2018-07-04, Last modification date: 2024-06-19) |
| Primary citation | Makrynitsa, G.I.,Ntonti, D.,Marousis, K.D.,Birkou, M.,Matsoukas, M.T.,Asami, S.,Bentrop, D.,Papageorgiou, N.,Canard, B.,Coutard, B.,Spyroulias, G.A. Conformational plasticity of the VEEV macro domain is important for binding of ADP-ribose. J.Struct.Biol., 206:119-127, 2019 Cited by PubMed Abstract: Venezuelan equine encephalitis virus (VEEV) is a new world alphavirus which can be involved in several central nervous system disorders such as encephalitis and meningitis. The VEEV genome codes for 4 non-structural proteins (nsP), of which nsP3 contains a Macro domain. Macro domains (MD) can be found as stand-alone proteins or embedded within larger proteins in viruses, bacteria and eukaryotes. Their most common feature is the binding of ADP-ribose (ADPr), while several macro domains act as ribosylation writers, erasers or readers. Alphavirus MD erase ribosylation but their precise contribution in viral replication is still under investigation. NMR-driven titration experiments of ADPr in solution with the VEEV macro domain (in apo- and complex state) show that it adopts a suitable conformation for ADPr binding. Specific experiments indicate that the flexibility of the loops β5-α3 and α3-β6 is critical for formation of the complex and assists a wrapping mechanism for ADPr binding. Furthermore, along with this sequence of events, the VEEV MD undergoes a conformational exchange process between the apo state and a low-populated "dark" conformational state. PubMed: 30825649DOI: 10.1016/j.jsb.2019.02.008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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