5Y2H
Crystal structure of the oligomerization domain of NSP4 from the rotavirus strain MF66
Summary for 5Y2H
| Entry DOI | 10.2210/pdb5y2h/pdb |
| Descriptor | Nonstructural protein 4 (2 entities in total) |
| Functional Keywords | antiparallel tetramer nsp4 rotavirus coiled-coil mf66, viral protein |
| Biological source | Bovine rotavirus G10 |
| Total number of polymer chains | 4 |
| Total formula weight | 24604.73 |
| 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 Cited by 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: 29455326DOI: 10.1007/s00705-018-3753-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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