6S2Z

Water-soluble Chlorophyll Protein (WSCP) from Brassica oleracea var. Botrytis with Chlorophyll-b

6S2Z の概要

• エントリーDOI: 10.2210/pdb6s2z/pdb
• 分子名称: Water-Soluble Chlorophyll Protein, CHLOROPHYLL B (3 entities in total)
• 機能のキーワード: tetramer, plant, brassica oleracea, chlorophyll, water-soluble chlorophyll protein, photooxidation, chlorophyll carrier, plant protein
• 由来する生物種: Brassica oleracea var. botrytis (Cauliflower)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20079.20

構造登録者

Agostini, A.,Meneghin, E.,Gewehr, L.,Pedron, D.,Palm, D.M.,Carbonera, D.,Paulsen, H.,Jaenicke, E.,Collini, E. (登録日: 2019-06-23, 公開日: 2019-12-18, 最終更新日: 2024-10-09)

主引用文献

Agostini, A.,Meneghin, E.,Gewehr, L.,Pedron, D.,Palm, D.M.,Carbonera, D.,Paulsen, H.,Jaenicke, E.,Collini, E.
How water-mediated hydrogen bonds affect chlorophyll a/b selectivity in Water-Soluble Chlorophyll Protein.
Sci Rep, 9:18255-18255, 2019

PubMed Abstract: The Water-Soluble Chlorophyll Protein (WSCP) of Brassicaceae is a remarkably stable tetrapyrrole-binding protein that, by virtue of its simple design, is an exceptional model to investigate the interactions taking place between pigments and their protein scaffold and how they affect the photophysical properties and the functionality of the complexes. We investigated variants of WSCP from Lepidium virginicum (Lv) and Brassica oleracea (Bo), reconstituted with Chlorophyll (Chl) b, to determine the mechanisms by which the different Chl binding sites control their Chl a/b specificities. A combined Raman and crystallographic investigation has been employed, aimed to characterize in detail the hydrogen-bond network involving the formyl group of Chl b. The study revealed a variable degree of conformational freedom of the hydrogen bond networks among the WSCP variants, and an unexpected mixed presence of hydrogen-bonded and not hydrogen-bonded Chls b in the case of the L91P mutant of Lv WSCP. These findings helped to refine the description of the mechanisms underlying the different Chl a/b specificities of WSCP versions, highlighting the importance of the structural rigidity of the Chl binding site in the vicinity of the Chl b formyl group in granting a strong selectivity to binding sites.

PubMed: 31796824
DOI: 10.1038/s41598-019-54520-4

実験手法

X-RAY DIFFRACTION (2.5 Å)