organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / electron transfer activity / iron ion binding / heme binding / metal ion binding / plasma membrane Similarity search - Function
Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain ...Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain / Antenna complex, beta domain superfamily / Antenna complex alpha/beta subunit / Light-harvesting complex / Photosynthetic reaction centre, M subunit / Photosynthetic reaction centre, L subunit / Multiheme cytochrome superfamily / : / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. Similarity search - Domain/homology
Antenna pigment protein beta chain / Antenna pigment protein alpha chain / Reaction center protein L chain / Reaction center protein M chain / Photosynthetic reaction center cytochrome c subunit Similarity search - Component
Biological species
Rhodovulum sulfidophilum DSM 1374 (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 1.81 Å
Journal: Commun Biol / Year: 2026 Title: Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum. Authors: Xing-Yu Yue / Guang-Lei Wang / Shinya Kosaki / Kenji V P Nagashima / Yu-Lu Wu / Yuki Kobayashi / Tomoya Sugiyama / Ryo Kanno / Endang R Purba / Shinichi Takaichi / Toshiaki Mochizuki / Akira ...Authors: Xing-Yu Yue / Guang-Lei Wang / Shinya Kosaki / Kenji V P Nagashima / Yu-Lu Wu / Yuki Kobayashi / Tomoya Sugiyama / Ryo Kanno / Endang R Purba / Shinichi Takaichi / Toshiaki Mochizuki / Akira Mizoguchi / Bruno M Humbel / Michael T Madigan / Hiroyuki Mino / Kazutoshi Tani / Yukihiro Kimura / Zheng-Yu Wang-Otomo / Long-Jiang Yu / Abstract: The marine purple nonsulfur phototrophic bacterium Rhodovulum (Rdv.) sulfidophilum (Alphaproteobacteria) has been a model organism for bacterial photosynthesis research because of its unusual ability ...The marine purple nonsulfur phototrophic bacterium Rhodovulum (Rdv.) sulfidophilum (Alphaproteobacteria) has been a model organism for bacterial photosynthesis research because of its unusual ability to grow phototrophically (anoxic/light) using high concentrations of inorganic or organic sulfur compounds as electron donors or by respiration under fully oxic conditions. Here we present a 1.81 Å-resolution cryo-EM structure of the light-harvesting 1-reaction center (LH1-RC) photocomplex from the Rdv. sulfidophilum type strain W4 with a focus on RC structure and function. The Rdv. sulfidophilum RC is characterized by its cytochrome (Cyt) subunit that contains three heme groups and is anchored by its intact N-terminal domain in the membrane. In contrast to a methionine as the 6th axial ligand to the heme-2 in other bacterial RC-bound triheme and tetraheme Cyt subunits, the outmost heme-2 in the Rdv. sulfidophilum Cyt subunit is ligated by a cysteine residue, resulting in a significant downshift of reduction potential of 470 mV compared to that of a methionine-ligated heme-2. A nonheme Fe ligated by a histidine of the Cyt subunit and five water molecules was identified in close proximity to heme-2, implying a potential role in electron transport from soluble electron donors to heme-2. The Rdv. sulfidophilum LH1 complex forms an open ring structure consisting of 16 αβ-subunits with a gap formed where the N-terminal transmembrane domain of the RC Cyt subunit and a newly identified protein with three helical domains (designated as protein-3h) are located. Protein-3h corresponds to the truncated N-terminal fragment of a gene product encoded by the pseudo-gene urf1 in the NADH:ubiquinone oxidoreductase (complex I) nuo operon in the genome of Rdv. sulfidophilum W4. Genes urf1 are also found in other purple nonsulfur bacteria and in aerobic anoxygenic phototrophic bacteria, and their putative products all share a common structural motif of N-terminal transmembrane U-shaped tandem helices. Based on structural and spectroscopic data, possible electron transfer pathways between the Rdv. sulfidophilum RC Cyt subunit and soluble electron donors and potential roles of protein-3h in the structural integrity of LH1-RC are discussed.
Macromolecule #1: Antenna pigment protein beta chain
Macromolecule
Name: Antenna pigment protein beta chain / type: protein_or_peptide / ID: 1 Details: The sequence of organism Rhodovulum sulfidophilum DSM 1374 is not available during the biocuration, replaced by Q9WXD9 temporarily. Number of copies: 16 / Enantiomer: LEVO
Macromolecule #2: Antenna pigment protein alpha chain
Macromolecule
Name: Antenna pigment protein alpha chain / type: protein_or_peptide / ID: 2 Details: The sequence of organism Rhodovulum sulfidophilum DSM 1374 is not available during the biocuration, replaced by Q9WXE0 temporarily. Number of copies: 16 / Enantiomer: LEVO
Name: Reaction center protein L chain / type: protein_or_peptide / ID: 5 Details: The sequence of organism Rhodovulum sulfidophilum DSM 1374 is not available during the biocuration, replaced by Q9WXE1 temporarily. Number of copies: 1 / Enantiomer: LEVO
Name: Reaction center protein M chain / type: protein_or_peptide / ID: 6 Details: The sequence of organism Rhodovulum sulfidophilum DSM 1374 is not available during the biocuration, replaced by Q9WXE2 temporarily. Number of copies: 1 / Enantiomer: LEVO
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