- EMDB-61095: Structure of photosynthetic LH1-RC complex from the purple bacter... -
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Basic information
Entry
Database: EMDB / ID: EMD-61095
Title
Structure of photosynthetic LH1-RC complex from the purple bacterium Blastochloris tepida
Map data
full-map
Sample
Complex: Photosynthetic LH1-RC complex of Blastochloris tepida
Protein or peptide: x 8 types
Ligand: x 14 types
Keywords
LH1-RC COMPLEX / PHOTOSYNTHESIS / PURPLE BACTERIA
Function / homology
Function and homology information
organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / endomembrane system / electron transfer activity / iron ion binding ...organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / endomembrane system / electron transfer activity / iron ion binding / heme binding / metal ion binding / membrane / 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, H subunit / Bacterial photosynthetic reaction centre, H-chain, C-terminal / Photosynthetic reaction centre, M subunit / Photosynthetic reaction centre, H subunit, N-terminal / Photosynthetic reaction centre, H subunit, N-terminal domain superfamily / Photosynthetic reaction centre, H-chain N-terminal region / PRC-barrel domain / PRC-barrel domain / Photosynthetic reaction centre, L subunit / PRC-barrel-like superfamily / Multiheme cytochrome superfamily / : / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. / Prokaryotic membrane lipoprotein lipid attachment site profile. Similarity search - Domain/homology
Photosynthetic reaction center subunit H / Antenna complex alpha/beta subunit domain-containing protein / Antenna complex alpha/beta subunit domain-containing protein / Reaction center protein L chain / Reaction center protein M chain / Photosynthetic reaction center cytochrome c subunit / Uncharacterized protein / Light-harvesting protein B-1015 gamma chain Similarity search - Component
Biological species
Blastochloris tepida (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 2.2 Å
Japan Agency for Medical Research and Development (AMED)
JP21am0101118
Japan
Japan Agency for Medical Research and Development (AMED)
JP21am0101116
Japan
Japan Society for the Promotion of Science (JSPS)
JP16H04174
Japan
Japan Society for the Promotion of Science (JSPS)
JP18H05153
Japan
Japan Society for the Promotion of Science (JSPS)
20H05086
Japan
Japan Society for the Promotion of Science (JSPS)
20H02856
Japan
Citation
Journal: Biochemistry / Year: 2025 Title: The Thermal-Stable LH1-RC Complex of a Hot Spring Purple Bacterium Powers Photosynthesis with Extremely Low-Energy Near-Infrared Light. Authors: Yukihiro Kimura / Ryo Kanno / Kaisei Mori / Yoshiki Matsuda / Ryuta Seto / Shinji Takenaka / Hiroyuki Mino / Tatsunari Ohkubo / Mai Honda / Yuji C Sasaki / Jun-Ichi Kishikawa / Kaoru ...Authors: Yukihiro Kimura / Ryo Kanno / Kaisei Mori / Yoshiki Matsuda / Ryuta Seto / Shinji Takenaka / Hiroyuki Mino / Tatsunari Ohkubo / Mai Honda / Yuji C Sasaki / Jun-Ichi Kishikawa / Kaoru Mitsuoka / Kazuhiro Mio / Malgorzata Hall / Endang R Purba / Toshiaki Mochizuki / Akira Mizoguchi / Bruno M Humbel / Michael T Madigan / Zheng-Yu Wang-Otomo / Kazutoshi Tani / Abstract: is a hot spring purple nonsulfur phototrophic bacterium that contains bacteriochlorophyll (BChl) . Here, we present a 2.21 Å cryo-EM structure of the thermostable light-harvesting 1-reaction center ... is a hot spring purple nonsulfur phototrophic bacterium that contains bacteriochlorophyll (BChl) . Here, we present a 2.21 Å cryo-EM structure of the thermostable light-harvesting 1-reaction center (LH1-RC) complex from . The LH1 ring comprises 16 circularly arranged αβγ-subunits plus one αβ-subunit that surround the RC complex composed of C-, H-, L-, and M-subunits. In a comparative study, the LH1-RC showed numerous electrostatic and hydrophobic interactions both within the LH1 complex itself and between the LH1 and the RC complexes that are absent from the LH1-RC complex of its mesophilic counterpart, . These additional interactions result in a tightly packed LH1-RC architecture with a reduced accessible surface area per volume that enhances the thermal stability of the complex and allows the light reactions of photosynthesis to proceed at hot spring temperatures. Moreover, based on high-resolution structural information combined with spectroscopic evidence, the unique photosynthetic property of the LH1-RC─absorption of energy-poor near-infrared light beyond 1000 nm─can be attributed to strong hydrogen-bonding interactions between the C3-acetyl C═O of the LH1 BChl and two LH1 α-Trp residues, structural rigidity of the LH1, and the enhanced exciton coupling of the LH1 BChls of this thermophile.
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