3MIW

Crystal Structure of Rotavirus NSP4

Summary for 3MIW

• Entry DOI: 10.2210/pdb3miw/pdb
• Related: 2o1j 2o1k
• Descriptor: Non-structural glycoprotein 4, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: rotavirus enterotoxin, non structural protein, nsp4, pentameric coiled coil, virulence, viral protein
• Biological source: Human rotavirus G4 (RV-A)
• Cellular location: Non-structural glycoprotein 4: Host rough endoplasmic reticulum membrane; Single-pass type III membrane protein (By similarity): Q82035
• Total number of polymer chains: 10
• Total formula weight: 66733.24

Authors

Chacko, A.R.,Read, R.J.,Dodson, E.J.,Rao, D.C.,Suguna, K. (deposition date: 2010-04-12, release date: 2011-05-25, Last modification date: 2024-02-21)

Primary citation

Chacko, A.R.,Jeyakanthan, J.,Ueno, G.,Sekar, K.,Rao, C.D.,Dodson, E.J.,Suguna, K.,Read, R.J.
A new pentameric structure of rotavirus NSP4 revealed by molecular replacement.
Acta Crystallogr.,Sect.D, 68:57-61, 2012

PubMed Abstract: The region spanning residues 95-146 of the rotavirus nonstructural protein NSP4 from the asymptomatic human strain ST3 has been purified and crystallized and diffraction data have been collected to a resolution of 2.6 Å. Several attempts to solve the structure by the molecular-replacement method using the available tetrameric structures of this domain were unsuccessful despite a sequence identity of 73% to the already known structures. A more systematic approach with a dimer as the search model led to an unexpected pentameric structure using the program Phaser. The various steps involved in arriving at this molecular-replacement solution, which unravelled a case of subtle variation between different oligomeric states unknown at the time of solving the structure, are presented in this paper.

PubMed: 22194333
DOI: 10.1107/S0907444911049705

Experimental method

X-RAY DIFFRACTION (2.5 Å)