Trimeric Domain-swapped Barnase

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1999 Feb 3

PMID 9927651

Citations 20

Authors

I Zegers

J DeSwarte

L Wyns

Affiliations

Soon will be listed here.

Abstract

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 A 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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