1e7n
From Proteopedia
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THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER
Overview
betagamma-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, betagamma-crystallin superfamily have not revealed a prototype ancestral, solution homodimer. Here we report the 2.35 A X-ray structure of the, homodimer of the N-terminal domain of rat betaB2-crystallin (betaB2-N)., The two identical domains pair in a symmetrical manner very similar to, that observed in native betagamma-crystallins, where N and C-terminal, domains (which share approximately 35% sequence identity) are related by a, pseudo-2-fold axis. betaB2-N thus resembles the ancestral prototype of the, betagamma-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 betagamma-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 betagamma-crystallin superfamily has evolved by a series, of gene duplication and fusion events from a single-domain ancestor, capable of forming homodimers.
About this Structure
1E7N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer., Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C, J Mol Biol. 2000 Dec 1;304(3):253-7. PMID:11090271
Page seeded by OCA on Tue Nov 20 13:49:02 2007
