5Y2E

Crystal structure of the oligomerization domain of NSP4 from the rotavirus strain NCDV

Summary for 5Y2E

• Entry DOI: 10.2210/pdb5y2e/pdb
• Descriptor: Non-structural glycoprotein 4 (2 entities in total)
• Functional Keywords: antiparallel tetramer nsp4 rotavirus coiled-coil, viral protein
• Biological source: Rotavirus A (strain RVA/Cow/United States/NCDV-Lincoln/1969/G6P6[1]) (RV-A)
• Cellular location: Host rough endoplasmic reticulum membrane ; Single-pass type III membrane protein : P08434
• Total number of polymer chains: 4
• Total formula weight: 22999.78

Authors

Suguna, K.,Kumar, S. (deposition date: 2017-07-25, release date: 2018-03-14, Last modification date: 2024-03-27)

Primary citation

Kumar, S.,Ramappa, R.,Pamidimukkala, K.,Rao, C.D.,Suguna, K.
New tetrameric forms of the rotavirus NSP4 with antiparallel helices.
Arch. Virol., 163:1531-1547, 2018

PubMed Abstract: Rotavirus nonstructural protein 4, the first viral enterotoxin to be identified, is a multidomain, multifunctional glycoprotein. Earlier, we reported a Ca-bound coiled-coil tetrameric structure of the diarrhea-inducing region of NSP4 from the rotavirus strains SA11 and I321 and a Ca-free pentameric structure from the rotavirus strain ST3, all with a parallel arrangement of α-helices. pH was found to determine the oligomeric state: a basic pH favoured a tetramer, whereas an acidic pH favoured a pentamer. Here, we report two novel forms of the coiled-coil region of NSP4 from the bovine rotavirus strains MF66 and NCDV. These crystallized at acidic pH, forming antiparallel coiled-coil tetrameric structures without any bound Ca ion. Structural and mutational studies of the coiled-coil regions of NSP4 revealed that the nature of the residue at position 131 (Tyr/His) plays an important role in the observed structural diversity.

PubMed: 29455326
DOI: 10.1007/s00705-018-3753-6

Experimental method

X-RAY DIFFRACTION (2.7 Å)