2MCD

Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 D94E mutant


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 900 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain.

Borin, B.N.Tang, W.Nice, T.J.McCune, B.T.Virgin, H.W.Krezel, A.M.

(2014) Proteins 82: 1200-1209

  • DOI: https://doi.org/10.1002/prot.24484
  • Primary Citation of Related Structures:  
    2MCD, 2MCH, 2MCK

  • PubMed Abstract: 

    Compact viral genomes such as those found in noroviruses, which cause significant enteric disease in humans, often encode only a few proteins, but affect a wide range of processes in their hosts and ensure efficient propagation of the virus. Both human and mouse noroviruses (MNVs) persistently replicate and are shed in stool, a highly effective strategy for spreading between hosts. For MNV, the presence of a glutamate rather than an aspartate at position 94 of the NS1/2 protein was previously shown to be essential for persistent replication and shedding. Here, we analyze these critical sequences of NS1/2 at the structural level. Using solution nuclear magnetic resonance methods, we determined folded NS1/2 domain structures from a nonpersistent murine norovirus strain CW3, a persistent strain CR6, and a persistent mutant strain CW3(D94E). We found an unstructured PEST-like domain followed by a novel folded domain in the N-terminus of NS1/2. All three forms of the domain are stable and monomeric in solution. Residue 94, critical for determining persistence, is located in a reverse turn following an α-helix in the folded domain. The longer side chain of glutamate, but not aspartate, allows interaction with the indole group of the nearby tryptophan, reshaping the surface of the domain. The discrimination between glutamyl and aspartyl residue is imposed by the stable tertiary conformation. These structural requirements correlate with the in vivo function of NS1/2 in persistence, a key element of norovirus biology and infection.


  • Organizational Affiliation

    NMR Accelerator, San Diego, California.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Murine norovirus 198Murine norovirus 1Mutation(s): 1 
Gene Names: NS1/2
UniProt
Find proteins for Q80J95 (Norovirus (isolate Mouse/NoV/United States/MNV1/2002/GV))
Explore Q80J95 
Go to UniProtKB:  Q80J95
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ80J95
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 900 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-12-18
    Type: Initial release
  • Version 1.1: 2014-02-12
    Changes: Database references
  • Version 1.2: 2014-06-25
    Changes: Database references
  • Version 1.3: 2017-02-22
    Changes: Other
  • Version 1.4: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.5: 2024-05-15
    Changes: Data collection, Database references