4OGQ

Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex

4OGQ の概要

• エントリーDOI: 10.2210/pdb4ogq/pdb
• 関連するPDBエントリー: 1Q90 1VF5 2E74 2E75 2E76 2ZT9 3CX5 4H0L 4H13 4H44
• 分子名称: Cytochrome b6, UNDECYL-MALTOSIDE, (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate, ... (26 entities in total)
• 機能のキーワード: electron transfer, plastocyanin, cytochrome c6, thylakoid membrane, electron transport
• 由来する生物種: Nostoc sp.; 詳細
• 細胞内の位置: Cellular thylakoid membrane; Multi-pass membrane protein (By similarity): P0A384 Q93SX1; Cellular thylakoid membrane; Single-pass membrane protein (By similarity): Q93SW9 Q93SX0 Q8YVQ2 P0A3Y1 P58246 P61048
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 126320.19

構造登録者

Hasan, S.S.,Cramer, W.A. (登録日: 2014-01-16, 公開日: 2014-05-14, 最終更新日: 2024-12-25)

主引用文献

Hasan, S.S.,Cramer, W.A.
Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex.
Structure, 22:1008-1015, 2014

PubMed Abstract: The role of lipids in the assembly, structure, and function of hetero-oligomeric membrane protein complexes is poorly understood. The dimeric photosynthetic cytochrome b6f complex, a 16-mer of eight distinct subunits and 26 transmembrane helices, catalyzes transmembrane proton-coupled electron transfer for energy storage. Using a 2.5 Å crystal structure of the dimeric complex, we identified 23 distinct lipid-binding sites per monomer. Annular lipids are proposed to provide a connection for super-complex formation with the photosystem-I reaction center and the LHCII kinase enzyme for transmembrane signaling. Internal lipids mediate crosslinking to stabilize the domain-swapped iron-sulfur protein subunit, dielectric heterogeneity within intermonomer and intramonomer electron transfer pathways, and dimer stabilization through lipid-mediated intermonomer interactions. This study provides a complete structure analysis of lipid-mediated functions in a multi-subunit membrane protein complex and reveals lipid sites at positions essential for assembly and function.

PubMed: 24931468
DOI: 10.1016/j.str.2014.05.004

実験手法

X-RAY DIFFRACTION (2.501 Å)