Structure of a small heat shock protein from wheat (Triticum aestivum) TaHsp16.9 (PDB GME1). Upper left: Cartoon model of the monomer. Upper right: Cartoon model of the dimer which forms the substructure of the oligomer. Lower left: Cartoon model of the native dodecamer. Lower right: Surface model of the dodecamer. Center: Movie of TaHsp16.9 structure. Ref: van Montfort, Basha, Friedrich, Slingsby & Vierling (2001) Nat. Struct. Biol. 8: 1025-1030.
This movie was generated in Pymol by Keith Ballard, a graduate student in the Molecular and Cellular Biology program. It shows the molecular organization of TaHSP 16.9 (1GME) in monomeric, dimeric and oligomeric (dodecamer) forms. The dimer is proposed to be the species responsible for binding denaturing client proteins to prevent irreversible aggregation in the cell during heat stress.