1LIA

CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION

1LIA の概要

• エントリーDOI: 10.2210/pdb1lia/pdb
• 分子名称: R-PHYCOERYTHRIN, PHYCOCYANOBILIN, PHYCOUROBILIN, ... (5 entities in total)
• 機能のキーワード: light harvesting protein
• 由来する生物種: Polysiphonia urceolata; 詳細
• 細胞内の位置: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side (By similarity): Q01921 Q01922
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 79075.78

構造登録者

Liang, D.C.,Jiang, T.,Chang, W.R. (登録日: 1996-01-29, 公開日: 1997-07-29, 最終更新日: 2024-11-13)

主引用文献

Chang, W.R.,Jiang, T.,Wan, Z.L.,Zhang, J.P.,Yang, Z.X.,Liang, D.C.
Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution.
J.Mol.Biol., 262:721-731, 1996

PubMed Abstract: The structure of R-phycoerythrin (R-PE) from Polysiphonia urceolata was determined at 2.8 A resolution. The crystals belong to space group R3 with unit cell dimensions of a = b = 189.8 A, c = 60.1 A. The subunit composition of R-PE is (alpha 2 beta 2)3 gamma. The three-dimensional structure of R-PE was solved by the multiple isomorphous replacement method. After several cycles of model building and refinement, the crystallographic R-factor of the final model is 18.0% with data from 10.0 to 2.8 A resolution. The four phycoerythrobilin chromophores alpha 84, alpha 140a, beta 84 and beta 155 in an (alpha beta) unit are each covalently bound to a cysteine residue through ring A. The phycourobilin chromophore is bound to cysteine beta 50 by ring A and bound to cysteine beta 61 by ring D. The ring A and ring D of phycourobilin deviate from the conjugate plane formed by ring B and ring C and the four rings form a boat-shaped structure. R-PE contains a 34 kDa gamma subunit that is assumed to lie in the central channel of the molecular disc (alpha 2 beta 2)3. The energy transfer and relationship between cysteine residues and chromophores are discussed.

PubMed: 8876649
DOI: 10.1006/jmbi.1996.0547

実験手法

X-RAY DIFFRACTION (2.8 Å)