2Y5I

S100Z from zebrafish in complex with calcium

2Y5I の概要

• エントリーDOI: 10.2210/pdb2y5i/pdb
• 分子名称: S100 CALCIUM BINDING PROTEIN Z, CALCIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: metal-binding protein, ef-hand, calcium regulation, oligomerisation, neuronal development, spine2, structural proteomics in europe 2, metal binding protein
• 由来する生物種: DANIO RERIO (ZEBRAFISH)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 68352.18

構造登録者

Moroz, O.V.,Bronstein, I.B.,Wilson, K.S. (登録日: 2011-01-13, 公開日: 2011-07-27, 最終更新日: 2023-12-20)

主引用文献

Moroz, O.V.,Bronstein, I.B.,Wilson, K.S.
The Crystal Structure of Zebrafish S100Z: Implications for Calcium-Promoted S100 Protein Oligomerisation.
J.Mol.Biol., 411:1072-, 2011

PubMed Abstract: 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.

PubMed: 21756915
DOI: 10.1016/J.JMB.2011.06.048

実験手法

X-RAY DIFFRACTION (2.03 Å)