1ALL

ALLOPHYCOCYANIN

1ALL の概要

• エントリーDOI: 10.2210/pdb1all/pdb
• 分子名称: ALLOPHYCOCYANIN, PHYCOCYANOBILIN, ... (4 entities in total)
• 機能のキーワード: light-harvesting protein, phycobiliprotein
• 由来する生物種: Arthrospira platensis; 詳細
• 細胞内の位置: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P72504 P72505
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35558.53

構造登録者

Brejc, K.,Ficner, R.,Huber, R.,Steinbacher, S. (登録日: 1995-03-01, 公開日: 1996-07-11, 最終更新日: 2024-06-05)

主引用文献

Brejc, K.,Ficner, R.,Huber, R.,Steinbacher, S.
Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution.
J.Mol.Biol., 249:424-440, 1995

PubMed Abstract: The phycobiliprotein allophycocyanin from the cyanobacterium Spirulina platensis has been isolated and crystallized. The crystals belong to space group P6(3)22 with cell constants a = b = 101.9 A, c = 130.6 A, alpha = beta = 90 degrees, gamma = 120 degrees, with one (alpha beta) monomer in the asymmetric unit. The three-dimensional structure of the (alpha beta) monomer was solved by multiple isomorphous replacement. The crystal structure has been refined in a cyclic manner by energy-restrained crystallographic refinement and model building. The conventional crystallographic R-factor of the final model is 19.6% with data from 8.0 to 2.3 A. The molecular structure of the subunits resembles other solved phycobiliprotein structures. In comparison to C-phycocyanin and b-phycoerythrin the major differences arise from deletions and insertions of segments involved in the protein-chromophore interactions. The stereochemistry of the alpha 84 and beta 84 chiral atoms are C(2)-R, C(3)-R and C(31)-R. The configuration (C(4)-Z, C(10)-Z and C(15)-Z) and the conformation (C(5)-anti, C(9)-syn and C(14)-anti) are equal for both chromophores.

PubMed: 7783202
DOI: 10.1006/jmbi.1995.0307

実験手法

X-RAY DIFFRACTION (2.3 Å)