2WSF

Improved Model of Plant Photosystem I

2WSF の概要

• エントリーDOI: 10.2210/pdb2wsf/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: AT3G54890, PHOTOSYSTEM I REACTION CENTER SUBUNIT III, CHLOROPLASTIC, PHOTOSYSTEM I REACTION CENTER SUBUNIT V, CHLOROPLASTIC, ... (26 entities in total)
• 機能のキーワード: photosynthesis, electron transfer, membrane proteins, large complexes
• 由来する生物種: ARABIDOPSIS THALIANA (THALE CRESS); 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 649035.98

構造登録者

Amunts, A.,Toporik, H.,Borovikov, A.,Nelson, N. (登録日: 2009-09-05, 公開日: 2009-11-17, 最終更新日: 2020-07-29)

主引用文献

Amunts, A.,Toporik, H.,Borovikova, A.,Nelson, N.
Structure determination and improved model of plant photosystem I.
J. Biol. Chem., 285:3478-3486, 2010

PubMed Abstract: Photosystem I functions as a sunlight energy converter, catalyzing one of the initial steps in driving oxygenic photosynthesis in cyanobacteria, algae, and higher plants. Functionally, Photosystem I captures sunlight and transfers the excitation energy through an intricate and precisely organized antenna system, consisting of a pigment network, to the center of the molecule, where it is used in the transmembrane electron transfer reaction. Our current understanding of the sophisticated mechanisms underlying these processes has profited greatly from elucidation of the crystal structures of the Photosystem I complex. In this report, we describe the developments that ultimately led to enhanced structural information of plant Photosystem I. In addition, we report an improved crystallographic model at 3.3-A resolution, which allows analysis of the structure in more detail. An improved electron density map yielded identification and tracing of subunit PsaK. The location of an additional ten beta-carotenes as well as five chlorophylls and several loop regions, which were previously uninterpretable, are now modeled. This represents the most complete plant Photosystem I structure obtained thus far, revealing the locations of and interactions among 17 protein subunits and 193 non-covalently bound photochemical cofactors. Using the new crystal structure, we examine the network of contacts among the protein subunits from the structural perspective, which provide the basis for elucidating the functional organization of the complex.

PubMed: 19923216
DOI: 10.1074/jbc.M109.072645

実験手法

X-RAY DIFFRACTION (3.48 Å)