Trimeric domain-swapped barnase

AUTOR(ES)

Zegers, Ingrid

FONTE

The National Academy of Sciences

RESUMO

The structure of a trimeric domain-swapped form of barnase (EC 3.1.27.3) was determined by x-ray crystallography at a resolution of 2.2 Å from crystals of space group R32. Residues 1–36 of one molecule associate with residues 41–110 from another molecule related through threefold symmetry. The resulting cyclic trimer contains three protein folds that are very similar to those in monomeric barnase. Both swapped domains contain a nucleation site for folding. The formation of a domain-swapped trimer is consistent with the description of the folding process of monomeric barnase as the formation and subsequent association of two foldons.

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