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Structure paper

TitleCryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae.
Journal, issue, pagesAdv Sci (Weinh), Vol. 12, Issue 18, Page e2413456, Year 2025
Publish dateMar 20, 2025
AuthorsWeiwei Wang / Yanting Liu / Jiayi Gu / Shaoya An / Cheng Ma / Haichun Gao / Nianzhi Jiao / Jian-Ren Shen / John Thomas Beatty / Michal Koblížek / Xing Zhang / Qiang Zheng / Jing-Hua Chen /
PubMed AbstractThe reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy ...The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy structure of the RC-LH1 isolated from a marine photoheterotrophic bacterium Dinoroseobacter shibae. The RC comprises four subunits, including a three-heme cytochrome (Cyt) c protein, and is surrounded by a closed LH ring composed of 17 pairs of antenna subunits. Notably, a novel subunit with an N-terminal "helix-turn-helix" motif embedded in the gap between the RC and the LH ring is identified. The purified RC-LH1 complex exhibits high stability in solutions containing Mg or Ca. The periplasmic Cyt c is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c to the proximal heme of the tri-heme Cyt, and subsequently to the special pair of bacteriochlorophylls. These findings provide structural insights into the efficient energy and electron transfer processes within a distinct type of RC-LH1, and shed light on evolutionary adaptations of photosynthesis.
External linksAdv Sci (Weinh) / PubMed:40112203 / PubMed Central
MethodsEM (single particle)
Resolution2.68 - 2.78 Å
Structure data

39671

8yy9

EMDB-39671, PDB-8yy9:
Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with magnesium-free solutions.
Method: EM (single particle) / Resolution: 2.7 Å

39683

8yz2

EMDB-39683, PDB-8yz2:
Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with magnesium solutions
Method: EM (single particle) / Resolution: 2.68 Å

62419

9km0

EMDB-62419, PDB-9km0:
Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na-containing solutions
Method: EM (single particle) / Resolution: 2.78 Å

Chemicals

ChemComp-BCL:
BACTERIOCHLOROPHYLL A

PDB-1efu:
ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-MW9:
(21R,24R,27S)-24,27,28-trihydroxy-18,24-dioxo-19,23,25-trioxa-24lambda~5~-phosphaoctacosan-21-yl (9Z)-octadec-9-enoate

ChemComp-FE:
Unknown entry

ChemComp-BPH:
BACTERIOPHEOPHYTIN A

ChemComp-U10:
UBIQUINONE-10

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-HEC:
HEME C

Source
  • dinoroseobacter shibae dfl 12 = dsm 16493 (bacteria)
KeywordsPHOTOSYNTHESIS / Reaction center / Energy transfer / Photosynthetic bacteria

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