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Protein Science, Vol 7, Issue 6 1280-1285, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Circular permutation of {beta}B2-crystallin changes the hierarchy of domain assembly

G. WRIGHT, A. K. BASAK, K. WIELIGMANN, E. M. MAYR and C. SLINGSBY
Birkbeck College, Department of Crystallography, Malet Street, London WC1E 7HX, United Kingdom

The {beta}{gamma}-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the {beta}B2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric {gamma}-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain {beta}B2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.
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