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J. Biol. Chem., Vol. 276, Issue 15, 12024-12029, April 13, 2001

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A Novel Quaternary Structure of the Dimeric -Crystallin Domain with Chaperone-like Activity^*

Ingeborg K. Feil^§, Marc Malfois, Jörg Hendle, Hans van der Zandt^¶, and Dmitri I. Svergun^**

From the  European Molecular Biology Laboratory (EMBL), EMBL Hamburg Outstation, Notkestrasse 85, D-22603 Hamburg, Germany, ^¶ EMBL, EMBL Heidelberg, Protein Expression and Purification Unit, Meyerhofsrasse 1, D-69012 Heidelberg, Germany, and  Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, 117333 Moscow, Russia

B-crystallin, a member of the small heat-shock protein family and a major eye lens protein, is a high molecular mass assembly and can act as a molecular chaperone. We report a synchrotron radiation x-ray solution scattering study of a truncation mutant from the human B-crystallin (B57-157), a dimeric protein that comprises the -crystallin domain of the B-crystallin and retains a significant chaperone-like activity. According to the sequence analysis (more than 23% identity), the monomeric fold of the -crystallin domain should be close to that of the small heat-shock protein from Methanococcus jannaschii (MjHSP16.5). The theoretical scattering pattern computed from the crystallographic model of the dimeric MjHSP16.5 deviates significantly from the experimental scattering by the -crystallin domain, pointing to different quaternary structures of the two proteins. A rigid body modeling against the solution scattering data yields a model of the -crystallin domain revealing a new dimerization interface. The latter consists of a strand-turn-strand motif contributed by each of the monomers, which form a four-stranded, antiparallel, intersubunit composite -sheet. This model agrees with the recent spin labeling results and suggests that the B-crystallin is composed by flexible building units with an extended surface area. This flexibility may be important for biological activity and for the formation of B-crystallin complexes of variable sizes and compositions.

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