7C52

Co-crystal structure of a photosynthetic LH1-RC in complex with electron donor HiPIP

Summary for 7C52

• Entry DOI: 10.2210/pdb7c52/pdb
• Related: 5D8V 5Y5S
• Descriptor: Photosynthetic reaction center cytochrome c subunit, GLYCEROL, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, ... (23 entities in total)
• Functional Keywords: lh1-rc, hipip, purple bacteria, electron transfer, photosynthesis
• Biological source: Thermochromatium tepidum; More
• Total number of polymer chains: 37
• Total formula weight: 424367.96

Authors

Yu, L.-J.,Wang-Otomo, Z.-Y. (deposition date: 2020-05-18, release date: 2021-03-03, Last modification date: 2023-11-29)

Primary citation

Kawakami, T.,Yu, L.J.,Liang, T.,Okazaki, K.,Madigan, M.T.,Kimura, Y.,Wang-Otomo, Z.Y.
Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP.
Nat Commun, 12:1104-1104, 2021

PubMed Abstract: Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems.

PubMed: 33597527
DOI: 10.1038/s41467-021-21397-9

Experimental method

X-RAY DIFFRACTION (2.89 Å)