1NWD

Solution Structure of Ca2+/Calmodulin bound to the C-terminal Domain of Petunia Glutamate Decarboxylase

1NWD の概要

• エントリーDOI: 10.2210/pdb1nwd/pdb
• NMR情報: BMRB: 5770
• 分子名称: Calmodulin, Glutamate decarboxylase, CALCIUM ION (3 entities in total)
• 機能のキーワード: calmodulin-peptide complex, calmodulin, gad, glutamate decarboxylase, dimer, binding protein-hydrolase complex, binding protein/hydrolase
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 23567.51

構造登録者

Yap, K.L.,Yuan, T.,Mal, T.K.,Vogel, H.J.,Ikura, M. (登録日: 2003-02-06, 公開日: 2003-04-08, 最終更新日: 2024-05-22)

主引用文献

Yap, K.L.,Yuan, T.,Mal, T.K.,Vogel, H.J.,Ikura, M.
Structural Basis for Simultaneous Binding of Two Carboxy-terminal Peptides of Plant Glutamate Decarboxylase to Calmodulin
J.Mol.Biol., 328:193-204, 2003

PubMed Abstract: Activation of glutamate decarboxylase (GAD) by calcium-bound calmodulin (CaM) is required for normal plant growth through regulation of gamma-aminobutyrate and glutamate metabolism. The interaction of CaM with the C-terminal domain of GAD is believed to induce dimerization of the enzyme, an event implicated for Ca(2+)-dependent enzyme activation. Here, we present the solution structure of CaM in complex with a dimer of peptides derived from the C-terminus of Petunia hybrida GAD. The 23 kDa ternary complex is pseudo-symmetrical with each domain of CaM bound to one of the two antiparallel GAD peptides, which form an X-shape with an interhelical angle of 60 degrees. To accommodate the dimeric helical GAD target, the two domains of CaM adopt an orientation markedly different from that seen in other CaM-target complexes. Although the dimeric GAD domain is much larger than previously studied CaM-binding peptides, the two CaM domains appear closer together and make a number of interdomain contacts not observed in earlier complexes. The present structure of a single CaM molecule interacting with two target peptides provides new evidence for the conformational flexibility of CaM as well as a structural basis for the ability of CaM to activate two enzyme molecules simultaneously.

PubMed: 12684008
DOI: 10.1016/S0022-2836(03)00271-7

実験手法

SOLUTION NMR