Trimeric domain-swapped barnase
- Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie, Paardenstraat 65, B-1640 St. Genesius Rode, Belgium
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Edited by David S. Eisenberg, University of California, Los Angeles, CA, and approved December 4, 1998 (received for review September 23, 1998)
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 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.
Footnotes
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↵ * To whom reprint requests should be addressed. e-mail: igzegers{at}vub.ac.be.
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This paper was submitted directly (Track II) to the Proceedings Office.
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Data deposition: The atomic coordinates have been deposited in the Protein Data Bank, Biology Department, Brookhaven National Laboratory, Upton, NY 11973 (PDB ID code 1yvs).
- Copyright © 1999, The National Academy of Sciences
