3O2C

Crystal structure of a rod form of c-phycocyanin from Themosynechococcus vulcanus at 1.5 angstroms

3O2C の概要

• エントリーDOI: 10.2210/pdb3o2c/pdb
• 関連するPDBエントリー: 1I7Y 1KTP 1ON7 3O18
• 分子名称: C-phycocyanin alpha subunit, C-phycocyanin beta subunit, PHYCOCYANOBILIN, ... (4 entities in total)
• 機能のキーワード: photosynthesis, phycobilisome, cyanobacteria, light harvesting
• 由来する生物種: Thermosynechococcus vulcanus (Synechococcus vulcanus); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37453.39

構造登録者

David, L.,Marx, A.,Adir, N. (登録日: 2010-07-22, 公開日: 2010-11-03, 最終更新日: 2025-03-26)

主引用文献

David, L.,Marx, A.,Adir, N.
High-resolution crystal structures of trimeric and rod phycocyanin.
J.Mol.Biol., 405:201-213, 2011

PubMed Abstract: The phycobilisome light-harvesting antenna in cyanobacteria and red algae is assembled from two substructures: a central core composed of allophycocyanin surrounded by rods that always contain phycocyanin (PC). Unpigmented proteins called linkers are also found within the rods and core. We present here two new structures of PC from the thermophilic cyanobacterium Thermosynechococcus vulcanus. We have determined the structure of trimeric PC to 1.35 Å, the highest resolution reported to date for this protein. We also present a structure of PC isolated in its intact and functional rod form at 1.5 Å. Analysis of rod crystals showed that in addition to the α and β PC subunit, there were three linker proteins: the capping rod linker (L(R)(8.7)), the rod linker (L(R)), and only one of three rod-core linkers (L(RC), CpcG4) with a stoichiometry of 12:12:1:1:1. This ratio indicates that the crystals contained rods composed of two hexamers. The crystallographic parameters of the rod crystals are nearly identical with that of the trimeric form, indicating that the linkers do not affect crystal packing and are completely embedded within the rod cavities. Absorption and fluorescence emission spectra were red-shifted, as expected for assembled rods, and this could be shown for the rod in solution as well as in crystal using confocal fluorescence microscopy. The crystal packing imparts superimposition of the three rod linkers, canceling out their electron density. However, analysis of B-factors and the conformations of residues facing the rod channel indicate the presence of linkers. Based on the experimental evidence presented here and a homology-based model of the L(R) protein, we suggest that the linkers do not in fact link between rod hexamers but stabilize the hexameric assembly and modify rod energy absorption and transfer capabilities.

PubMed: 21035460
DOI: 10.1016/j.jmb.2010.10.036

実験手法

X-RAY DIFFRACTION (1.5 Å)