5UI2

CRYSTAL STRUCTURE OF ORANGE CAROTENOID PROTEIN

「1M98」から置き換えられました

5UI2 の概要

• エントリーDOI: 10.2210/pdb5ui2/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Orange carotenoid-binding protein, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: carotenoid binding protein
• 由来する生物種: Arthrospira maxima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72293.64

構造登録者

KERFELD, C.A.,SAWAYA, M.R.,VISHNU, B.,KROGMANN, D.,YEATES, T.O. (登録日: 2017-01-12, 公開日: 2017-01-25, 最終更新日: 2024-03-06)

主引用文献

Kerfeld, C.A.,Sawaya, M.R.,Brahmandam, V.,Cascio, D.,Ho, K.K.,Trevithick-Sutton, C.C.,Krogmann, D.W.,Yeates, T.O.
The crystal structure of a cyanobacterial water-soluble carotenoid binding protein.
Structure, 11:55-65, 2003

PubMed Abstract: Carotenoids undergo a wide range of photochemical reactions in animal, plant, and microbial systems. In photosynthetic organisms, in addition to light harvesting, they perform an essential role in protecting against light-induced damage by quenching singlet oxygen, superoxide anion radicals, or triplet-state chlorophyll. We have determined the crystal structure of a water-soluble orange carotenoid protein (OCP) isolated from the cyanobacterium Arthrospira maxima at a resolution of 2.1 A. OCP forms a homodimer with one carotenoid molecule per monomer. The carotenoid binding site is lined by a striking number of methionine residues. The structure reveals several possible ways in which the protein environment influences the spectral properties of the pigment and provides insight into how the OCP carries out its putative functions in photoprotection.

PubMed: 12517340

実験手法

X-RAY DIFFRACTION (2.1 Å)