1KN1

Crystal structure of allophycocyanin

1KN1 の概要

• エントリーDOI: 10.2210/pdb1kn1/pdb
• 分子名称: Allophycocyanin, PHYCOCYANOBILIN, ... (4 entities in total)
• 機能のキーワード: helix-turn-helix, electron transport
• 由来する生物種: Porphyra yezoensis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36020.98

構造登録者

Liang, D.C.,Liu, J.Y.,Jiang, T.,Zhang, J.P.,Chang, W.R. (登録日: 2001-12-18, 公開日: 2002-12-18, 最終更新日: 2024-10-23)

主引用文献

Liu, J.Y.,Jiang, T.,Zhang, J.P.,Liang, D.C.
Crystal structure of Allophycocyanin from red algae Porphyra yezoensis at 2.2 A resolution
J.BIOL.CHEM., 274:16945-16952, 1999

PubMed Abstract: The crystal structure of allophycocyanin from red algae Porphyra yezoensis (APC-PY) at 2.2-A resolution has been determined by the molecular replacement method. The crystal belongs to space group R32 with cell parameters a = b = 105.3 A, c = 189.4 A, alpha = beta = 90 degrees, gamma = 120 degrees. After several cycles of refinement using program X-PLOR and model building based on the electron density map, the crystallographic R-factor converged to 19.3% (R-free factor is 26.9%) in the range of 10.0 to 2.2 A. The r.m.s. deviations of bond length and angles are 0.015 A and 2.9 degrees, respectively. In the crystal, two APC-PY trimers associate face to face into a hexamer. The assembly of two trimers within the hexamer is similar to that of C-phycocyanin (C-PC) and R-phycoerythrin (R-PE) hexamers, but the assembly tightness of the two trimers to the hexamer is not so high as that in C-PC and R-PE hexamers. The chromophore-protein interactions and possible pathway of energy transfer were discussed. Phycocyanobilin 1alpha84 of APC-PY forms 5 hydrogen bonds with 3 residues in subunit 2beta of another monomer. In R-PE and C-PC, chromophore 1alpha84 only forms 1 hydrogen bond with 2beta77 residue in subunit 2beta. This result may support and explain great spectrum difference exists between APC trimer and monomer.

PubMed: 10358042
DOI: 10.1074/jbc.274.24.16945

実験手法

X-RAY DIFFRACTION (2.2 Å)