1e7n
From Proteopedia
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'''THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER''' | '''THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER''' | ||
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[[Category: Wieligmann, K.]] | [[Category: Wieligmann, K.]] | ||
[[Category: 2-fold symmetry]] | [[Category: 2-fold symmetry]] | ||
| - | [[Category: | + | [[Category: Crystallin]] |
| - | [[Category: | + | [[Category: Domain interaction]] |
| - | [[Category: | + | [[Category: Eye lens]] |
| - | [[Category: | + | [[Category: Protein structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:45:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:45, 2 May 2008
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 Fri May 2 14:45:58 2008
