1S6I

Ca2+-regulatory region (CLD) from soybean calcium-dependent protein kinase-alpha (CDPK) in the presence of Ca2+ and the junction domain (JD)

1S6I の概要

• エントリーDOI: 10.2210/pdb1s6i/pdb
• 関連するPDBエントリー: 1S6J
• NMR情報: BMRB: 6104
• 分子名称: Calcium-dependent protein kinase SK5, CALCIUM ION (2 entities in total)
• 機能のキーワード: ef-hand; helix-loop-helix; calcium-binding; calmodulin superfamily, transferase, plant protein
• 由来する生物種: Glycine max (soybean)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21420.96

構造登録者

Weljie, A.M.,Vogel, H.J. (登録日: 2004-01-23, 公開日: 2004-06-15, 最終更新日: 2024-05-22)

主引用文献

Weljie, A.M.,Vogel, H.J.
Unexpected structure of the Ca2+-regulatory region from soybean calcium-dependent protein kinase-alpha
J.Biol.Chem., 279:35494-35502, 2004

PubMed Abstract: Calcium-dependent protein kinases (CDPKs) are an extensive class of multidomain Ca(2+)-regulated enzymes from plants and protozoa. In vivo the so-called calmodulin-like domain (CLD) of CDPK binds intramolecularly to the junction domain (JD), which exhibits both kinase-inhibitory and CLD binding properties. Here we report the high resolution solution structure of the calcium-regulatory region from soybean CDPK-alpha determined in the presence of a peptide encompassing the JD. The structure of both lobes of CLD resembles that of related helix-loop-helix Ca(2+)-binding proteins. NMR chemical shift mapping studies demonstrate that the JD induces significant structural changes in isolated Ca(2+)-CLD, particularly the C-terminal domain, although a stable complex is not formed. A CLD solution structure calculated on the basis of NMR data and long range fluorescence resonance energy transfer distances reveals an activated state with both lobes positioned side by side, similar to calcineurin B rather than calmodulin, highlighting the possible pitfall of assigning function purely from sequence information.

PubMed: 15155727
DOI: 10.1074/jbc.M311520200

実験手法

SOLUTION NMR