1C7V

NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS

1C7V の概要

• エントリーDOI: 10.2210/pdb1c7v/pdb
• 関連するPDBエントリー: 1C7W
• 分子名称: CALCIUM VECTOR PROTEIN (1 entity in total)
• 機能のキーワード: ef-hand family, calcium binding protein, metal binding protein
• 由来する生物種: Branchiostoma lanceolatum (amphioxus)
• 細胞内の位置: Cytoplasm: P04573
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9279.27

構造登録者

Theret, I.,Baladi, S.,Cox, J.A.,Sakamoto, H.,Craescu, C.T. (登録日: 2000-03-27, 公開日: 2000-04-12, 最終更新日: 2023-12-27)

主引用文献

Theret, I.,Baladi, S.,Cox, J.A.,Sakamoto, H.,Craescu, C.T.
Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement.
Biochemistry, 39:7920-7926, 2000

PubMed Abstract: Calcium vector protein (CaVP) from amphioxus is a two-domain, calcium-binding protein (18.3 kDa) of the calmodulin superfamily. Only two of the four EF-hand motifs (sites III and IV) have a significant binding affinity for calcium ions. We determined the solution structure of the domain containing these active sites (C-CaVP: W81-S161), in the Ca(2+)-saturated state, using NMR spectroscopy and restrained molecular dynamics. The tertiary structure is similar to other Ca(2+)-binding domains containing a pair of EF-hand motifs. The apo state has spectroscopic and thermodynamic characteristics of a molten globule, with conserved secondary structure but highly fluctuating tertiary organization. Titration of C-CaVP with Ca(2+) revealed a stepwise ion binding, with a stable equilibrium intermediate in which only site III binds a calcium ion. Despite a highly fluctuating structure of the free site IV, the calcium-bound site III has a persistent structure, with similar secondary elements but different interhelix angle and hydrophobic packing relative to the fully calcium-saturated state.

PubMed: 10891072
DOI: 10.1021/bi000360z

実験手法

SOLUTION NMR