1KNZ

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer

Summary for 1KNZ

• Entry DOI: 10.2210/pdb1knz/pdb
• Descriptor: 5'-R(*UP*GP*AP*CP*C)-3', Nonstructural RNA-binding Protein 34 (3 entities in total)
• Functional Keywords: protein-ssrna complex, viral protein-rna complex, viral protein/rna
• Biological source: Simian rotavirus A/SA11
• Total number of polymer chains: 12
• Total formula weight: 153223.97

Authors

Deo, R.C.,Groft, C.M.,Rajashankar, K.R.,Burley, S.K. (deposition date: 2001-12-19, release date: 2002-01-17, Last modification date: 2024-02-14)

Primary citation

Deo, R.C.,Groft, C.M.,Rajashankar, K.R.,Burley, S.K.
Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer.
Cell(Cambridge,Mass.), 108:71-81, 2002

PubMed Abstract: Rotaviruses, the cause of life-threatening diarrhea in humans and cattle, utilize a functional homolog of poly(A) binding protein (PABP) known as nonstructural protein 3 (NSP3) for translation of viral mRNAs. NSP3 binds to viral mRNA 3' consensus sequences and circularizes the mRNA via interactions with eIF4G. The X-ray structure of the NSP3 RNA binding domain bound to a rotaviral mRNA 3' end has been determined. NSP3 is a novel, heart-shaped homodimer with a medial RNA binding cleft. The homodimer is asymmetric, and contains two similar N-terminal segments plus two structurally different C-terminal segments that intertwine to create a tunnel enveloping the mRNA 3' end. Biophysical studies demonstrate high affinity binding leading to increased thermal stability and slow dissociation kinetics, consistent with NSP3 function.

PubMed: 11792322
DOI: 10.1016/S0092-8674(01)00632-8

Experimental method

X-RAY DIFFRACTION (2.45 Å)