Abstract
beta gamma -crystallins from the eye lens are proteins consisting of two similar domains joined by a short linker. All three-dimensional structures of native proteins solved so far reveal similar pseudo-2-fold pairing of the domains reflecting their presumed ancient origin from a single-domain homodimer. However, studies of engineered single domains of members of the beta gamma -crystallin ...
Abstract
beta gamma -crystallins from the eye lens are proteins consisting of two similar domains joined by a short linker. All three-dimensional structures of native proteins solved so far reveal similar pseudo-2-fold pairing of the domains reflecting their presumed ancient origin from a single-domain homodimer. However, studies of engineered single domains of members of the beta gamma -crystallin superfamily have not revealed a prototype ancestral solution homodimer. Here we report the 2.35 Angstrom X-ray structure of the homodimer of the N-terminal domain of rat beta B2-crystallin (beta B2-N). The two identical domains pair in a symmetrical manner very similar to that observed in native beta gamma -crystallins, where N and C-terminal domains (which share similar to 35% sequence identity) are related by a pseudo-2-fold axis. beta B2-N thus resembles the ancestral prototype of the beta gamma -crystallin superfamily as it self-associates in solution to form a dimer with an essentially identical domain interface as that between the N and C domains in beta gamma -crystallins, but without the benefit of a covalent linker. The structure provides further evidence for the role of two-domain pairing in stabilising the protomer fold. These results support the view that the beta gamma -crystallin superfamily has evolved by a series of gene duplication and fusion events from a single-domain ancestor capable of forming homodimers. (C) 2000 Academic Press.
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