The Crystal Structure of Zebrafish S100Z: Implications for Calcium-Promoted S100 Protein Oligomerisation
| Autor: | Keith S. Wilson, Olga V. Moroz, Igor B. Bronstein |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Protein Conformation Molecular Sequence Data Danio chemistry.chemical_element Model system Crystal structure Calcium Crystallography X-Ray Antiparallel (biochemistry) S100 protein Structural Biology Animals Humans Amino Acid Sequence Molecular Biology Zebrafish Sequence Homology Amino Acid biology S100 Proteins biology.organism_classification Bony fish Crystallography chemistry Biophysics Protein Multimerization |
| Zdroj: | Journal of Molecular Biology. 411:1072-1082 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2011.06.048 |
| Popis: | The S100 family, with about 20 members in humans, is composed of EF-hand calcium-regulated proteins and is linked to a range of serious human diseases, including cancer and autoimmune and neurological disorders. The oldest S100 family members are found in teleosts (bony fish). The zebrafish, Danio rerio, was suggested as a promising model system for in vivo studies on S100 family functions, and we chose to investigate zebrafish S100Z as the closest homologue of the metastasis-promoting human S100A4. Here, we report the first crystal structure of an S100 protein from this organism, the calcium-bound state of S100Z to 2.03 Å resolution. Crystal packing suggests higher-order oligomerisation of S100Z dimers, with a tetramerisation interface very similar to, but even more extensive than, that reported for S100A4. The interactions are primarily through the C-terminal αIV helices from adjacent dimers in an antiparallel orientation. Structural comparisons between known S100 multimeric assemblies together with analysis of calcium-driven changes to the dimerisation cores suggest a mechanism for calcium-promoted oligomerisation of S100 proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect