3EVV

Crystal Structure of Calcium bound dimeric GCAMP2 (#2)

3EVV の概要

• エントリーDOI: 10.2210/pdb3evv/pdb
• 関連するPDBエントリー: 3EVP 3EVR 3EVU
• 分子名称: Myosin light chain kinase, Green fluorescent protein, Calmodulin chimera, CALCIUM ION (3 entities in total)
• 機能のキーワード: gcamp2, calcium sensor, gfp, calmodulin, m13, signaling protein
• 由来する生物種: Aequorea victoria (Jellyfish); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle : P0DP23
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51467.49

構造登録者

Wang, Q.,Shui, B.,Kotlikoff, M.I.,Sondermann, H. (登録日: 2008-10-13, 公開日: 2008-12-09, 最終更新日: 2023-12-27)

主引用文献

Wang, Q.,Shui, B.,Kotlikoff, M.I.,Sondermann, H.
Structural Basis for Calcium Sensing by GCaMP2.
Structure, 16:1817-1827, 2008

PubMed Abstract: Genetically encoded Ca(2+) indicators are important tools that enable the measurement of Ca(2+) dynamics in a physiologically relevant context. GCaMP2, one of the most robust indicators, is a circularly permutated EGFP (cpEGFP)/M13/calmodulin (CaM) fusion protein that has been successfully used for studying Ca(2+) fluxes in vivo in the heart and vasculature of transgenic mice. Here we describe crystal structures of bright and dim states of GCaMP2 that reveal a sophisticated molecular mechanism for Ca(2+) sensing. In the bright state, CaM stabilizes the fluorophore in an ionized state similar to that observed in EGFP. Mutational analysis confirmed critical interactions between the fluorophore and elements of the fused peptides. Solution scattering studies indicate that the Ca(2+)-free form of GCaMP2 is a compact, predocked state, suggesting a molecular basis for the relatively rapid signaling kinetics reported for this indicator. These studies provide a structural basis for the rational design of improved Ca(2+)-sensitive probes.

PubMed: 19081058
DOI: 10.1016/j.str.2008.10.008

実験手法

X-RAY DIFFRACTION (2.6 Å)