CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4
Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site.
PEG400, magnesium sulfate, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
NON-STRUCTURAL GLYCOPROTEIN NSP4 complexed with STRONTIUM ION
This sequence is derived from NSP4 from Simian 11 rotavirus (strain SA11).
Four water molecules have been modelled above the metal and hydrating water molecules. It is also possible that the four water molecules (two per ASU) are instead a small molecule lying across the two-fold crystallographic axis. There are two residues whose side chains have alternative rotomer conformations and have been modelled as such: B106 and B112.
The biological assembly is a tetramer which can be generated from chains A and B by constructing symmetry mates across the two-fold.
NS28, parallel coiled-coil, homo-tetramer, metal binding site, METAL BINDING PROTEIN