2DRE

Crystal structure of Water-soluble chlorophyll protein from lepidium virginicum at 2.00 angstrom resolution

2DRE の概要

• エントリーDOI: 10.2210/pdb2dre/pdb
• 分子名称: Water-soluble chlorophyll protein, CHLOROPHYLL A (3 entities in total)
• 機能のキーワード: beta-trefoil, tetramer, plant, lepidium virginicum, chlorophyll, water-soluble chlorophyll protein, singlet oxygen, photooxidation, chlorophyll carrier, kunitz (sti) inhibitors, plant protein
• 由来する生物種: Lepidium virginicum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 81940.06

構造登録者

Horigome, D.,Satoh, H.,Itoh, N.,Mitsunaga, K.,Oonishi, I.,Nakagawa, A.,Uchida, A. (登録日: 2006-06-08, 公開日: 2006-12-26, 最終更新日: 2024-11-13)

主引用文献

Horigome, D.,Satoh, H.,Itoh, N.,Mitsunaga, K.,Oonishi, I.,Nakagawa, A.,Uchida, A.
Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein.
J.Biol.Chem., 282:6525-6531, 2007

PubMed Abstract: A water-soluble chlorophyll-binding protein (WSCP) is the single known instance of a putative chlorophyll (Chl) carrier in green plants. Recently the photoprotective function of WSCP has been demonstrated by EPR measurements; the light-induced singlet-oxygen formation of Chl in the WSCP tetramer is about four times lower than that of unbound Chl. This paper describes the crystal structure of the WSCP-Chl complex purified from leaves of Lepidium virginicum (Virginia pepperweed) to clarify the mechanism of its photoprotective function. The WSCP-Chl complex is a homotetramer comprising four protein chains of 180 amino acids and four Chl molecules. At the center of the complex one hydrophobic cavity is formed in which all of the four Chl molecules are tightly packed and isolated from bulk solvent. With reference to the novel Chl-binding mode, we propose that the photoprotection mechanism may be based on the inhibition of physical contact between the Chl molecules and molecular oxygen.

PubMed: 17170107
DOI: 10.1074/jbc.M609458200

実験手法

X-RAY DIFFRACTION (2 Å)