The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins
| Autor: | Eva-Maria Mayr, Rudi Glockshuber, O. A. Bateman, Christine Slingsby, H.P.C. Driessen, B.V. Norledge, Rainer Jaenicke |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Macromolecular Substances Molecular Sequence Data Protein domain Sequence (biology) Crystal structure Biology Crystallography X-Ray Protein Engineering Biochemistry Protein Structure Secondary Domain (software engineering) Structural Biology Crystallin Genetics Animals Amino Acid Sequence Single domain Protein engineering Biological Evolution Crystallins Peptide Fragments Models Structural Molecular Weight Crystallography Pairing Cattle sense organs Crystallization |
| Zdroj: | Nature Structural Biology. 3:267-274 |
| ISSN: | 1072-8368 |
| DOI: | 10.1038/nsb0396-267 |
| Popis: | We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice. |
| Databáze: | OpenAIRE |
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