Palme, Stefan and Jaenicke, Rainer and Slingsby, Christine (1998) Unusual domain pairing in a mutant of bovine lens gamma B-crystallin. JOURNAL OF MOLECULAR BIOLOGY, 279 (5). pp. 1053-1059. ISSN 0022-2836, 1089-8638
Full text not available from this repository.Abstract
beta gamma-Crystallins from the eye lens are proteins consisting of two domains joined by a short linker. AU 3D structures solved so far reveal a similar pseudo-2-fold pairing of the domains, reflecting their presumed ancient origin from a single-domain homodimer. Here we report the 2.2 Angstrom X-ray structure of the N-terminal domain of gamma beta-crystallin, bearing a mutation of a residue involved in domain contacts in the native molecule (Phe56Ala). It forms a crystallographic homodimer, yet the domain orientation is different from native beta gamma-crystallins. It is considered that the new orientation derives from two structural features. (1) The replacement of the bulky phenylalanine 56 by an alanine results in a different optimal hydrophobic packing of interface residues between identical domains. (2) The paired domains have extensions derived from the domain Linker, each containing a proline conserved in gamma-crystallins, and the resulting steric constraints preclude a native-like pairing but support the new arrangement. These data highlight the pivotal role of interface residues and sequence extensions in overall domain assembly. (C) 1998 Academic Press.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | EYE LENS; PROTEINS; EVOLUTION; BETA-B2-CRYSTALLIN; PEPTIDE; crystallins; X-ray crystallography; protein structure; domain interactions; proline |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 24 Feb 2023 06:24 |
| Last Modified: | 24 Feb 2023 06:24 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49728 |
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