Clout, Naomi J. and Basak, Ajit and Wieligmann, Karin and Bateman, Orval A. and Jaenicke, Rainer and Slingsby, Christine (2000) The N-terminal domain of beta B2-crystallin resembles the putative ancestral homodimer. JOURNAL OF MOLECULAR BIOLOGY, 304 (3). pp. 253-257. ISSN 0022-2836
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | X-RAY-ANALYSIS; EYE LENS; CRYSTALLIN; PROTEINS; EVOLUTION; TRANSPARENCY; STABILITY; MUTANT; MODEL; crystallins; eye lens; protein structure; domain interactions; 2-fold symmetry |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Mar 2022 14:42 |
| Last Modified: | 14 Mar 2022 14:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/42015 |
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