1NG7

The Solution Structure of the Soluble Domain of Poliovirus 3A Protein

Summary for 1NG7

• Entry DOI: 10.2210/pdb1ng7/pdb
• NMR Information: BMRB: 5753
• Descriptor: Genome polyprotein [Core protein P3A] (1 entity in total)
• Functional Keywords: helical hairpin, unfolded domain, symmetric dimer, viral protein
• Biological source: Human poliovirus 1
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03300
• Total number of polymer chains: 2
• Total formula weight: 13823.69

Authors

Strauss, D.M.,Glustrom, L.W.,Wuttke, D.S. (deposition date: 2002-12-16, release date: 2003-07-15, Last modification date: 2024-05-22)

Primary citation

Strauss, D.M.,Glustrom, L.W.,Wuttke, D.S.
Towards an understanding of the poliovirus replication complex: the solution structure of the soluble domain of the poliovirus 3A protein.
J.Mol.Biol., 330:225-234, 2003

PubMed Abstract: Poliovirus is a positive-strand RNA virus and the prototypical member of the Picornaviridae family. Upon infection, the viral RNA genome is translated from a single open reading frame into a polypeptide which undergoes a series of cleavages to ultimately form four structural and seven non-structural proteins. A replication complex is then formed which replicates the viral genome into negative and positive strands for further translation, replication, and packaging into viral progeny. Poliovirus 3A protein (3A) is a critical component of the viral replication complex and is the putative target of enviroxime, an antiviral drug shown to block viral replication. 3A also inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport, a function which may play a key role in viral evasion from the host immune response. 3A, an 87-residue protein consisting of a soluble N terminus and a hydrophobic C terminus, is formed by the cleavage of the precursor protein 3AB into 3A and 3B (VPg). Although they differ by only 22 residues, the precursor protein 3AB and its cleavage product 3A have distinct functions in viral replication. We have determined the structure of the soluble, N-terminal domain of 3A (3A-N) using NMR spectroscopy. We show that 3A-N exists as a symmetric dimer, and each monomer consists of an alpha-helical hairpin with unstructured, yet functional, N- and C termini. We also show that the 3A-N structure contains a negatively charged surface patch and provides a context for interpreting the biochemical characteristics of a number of previously reported 3A and 3AB mutants.

PubMed: 12823963
DOI: 10.1016/S0022-2836(03)00577-1

Experimental method

SOLUTION NMR