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- EMDB-35989: Cryo-EM structure of native RC-LH complex from Roseiflexus casten... -

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Basic information

Entry
Database: EMDB / ID: EMD-35989
TitleCryo-EM structure of native RC-LH complex from Roseiflexus castenholzii at 2,000lux
Map data
Sample
  • Complex: the native RC-LH complex at 2,000lux
    • Protein or peptide: x 8 types
  • Ligand: x 7 types
KeywordsRC-LH core complex / PHOTOSYNTHESIS
Function / homology
Function and homology information


organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / chlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / electron transfer activity / iron ion binding / heme binding ...organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / chlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / electron transfer activity / iron ion binding / heme binding / membrane / 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 domain superfamily / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta subunit ...Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta domain superfamily / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta 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
Uncharacterized protein / Reaction center protein L chain / Alpha subunit of light-harvesting 1 / Beta subunit of light-harvesting 1
Similarity search - Component
Biological speciesRoseiflexus castenholzii DSM 13941 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsXu X / Xin J
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Elife / Year: 2023
Title: Carotenoid assembly regulates quinone diffusion and the reaction center-light harvesting complex architecture.
Authors: Jiyu Xin / Yang Shi / Xin Zhang / Xinyi Yuan / Yueyong Xin / Huimin He / Jiejie Shen / Robert E Blankenship / Xiaoling Xu /
Abstract: Carotenoid (Car) pigments perform central roles in photosynthesis-related light harvesting (LH), photoprotection, and assembly of functional pigment-protein complexes. However, the relationships ...Carotenoid (Car) pigments perform central roles in photosynthesis-related light harvesting (LH), photoprotection, and assembly of functional pigment-protein complexes. However, the relationships between Car depletion in the LH, assembly of the prokaryotic reaction center (RC)-LH complex, and quinone exchange are not fully understood. Here, we analyzed native RC-LH (nRC-LH) and Car-depleted RC-LH (dRC-LH) complexes in , a chlorosome-less filamentous anoxygenic phototroph that forms the deepest branch of photosynthetic bacteria. Newly identified exterior Cars functioned with the bacteriochlorophyll B800 to block the proposed quinone channel between LHαβ subunits in the nRC-LH, forming a sealed LH ring that was disrupted by transmembrane helices from cytochrome and subunit X to allow quinone shuttling. dRC-LH lacked subunit X, leading to an exposed LH ring with a larger opening, which together accelerated the quinone exchange rate. We also assigned amino acid sequences of subunit X and two hypothetical proteins Y and Z that functioned in forming the quinone channel and stabilizing the RC-LH interactions. This study reveals the structural basis by which Cars assembly regulates the architecture and quinone exchange of bacterial RC-LH complexes. These findings mark an important step forward in understanding the evolution and diversity of prokaryotic photosynthetic apparatus.
History
DepositionApr 24, 2023-
Header (metadata) releaseSep 20, 2023-
Map releaseSep 20, 2023-
UpdateOct 4, 2023-
Current statusOct 4, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35989.png

Downloads & links

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Map

FileDownload / File: emd_35989.map.gz / Format: CCP4 / Size: 70.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.893 Å
Density
Contour LevelBy AUTHOR: 0.015
Minimum - Maximum-0.050717916 - 0.10677596
Average (Standard dev.)0.00041391072 (±0.0048840665)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions264264264
Spacing264264264
CellA=B=C: 235.752 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_35989_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_35989_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : the native RC-LH complex at 2,000lux

EntireName: the native RC-LH complex at 2,000lux
Components
  • Complex: the native RC-LH complex at 2,000lux
    • Protein or peptide: Beta subunit of light-harvesting 1
    • Protein or peptide: Alpha subunit of light-harvesting 1
    • Protein or peptide: MULTIHEME_CYTC DOMAIN-CONTAINING PROTEIN
    • Protein or peptide: Reaction center protein L chainPhotosynthetic reaction centre
    • Protein or peptide: Reaction center protein M chainPhotosynthetic reaction centre
    • Protein or peptide: Subunit X
    • Protein or peptide: Subunit Y
    • Protein or peptide: Subunit Z
  • Ligand: BACTERIOCHLOROPHYLL ABacteriochlorophyll
  • Ligand: beta,psi-caroten-4-one
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: BACTERIOPHEOPHYTIN B
  • Ligand: 2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E,30E,34E,38E)-3,7,11,15,19,23,27,31,35,39,43-undecamethyltetratetraconta-2,6,10,1 4,18,22,26,30,34,38,42-undecaen-1-yl]naphthalene-1,4-dione
  • Ligand: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE
  • Ligand: FE (III) ION

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Supramolecule #1: the native RC-LH complex at 2,000lux

SupramoleculeName: the native RC-LH complex at 2,000lux / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)

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Macromolecule #1: Beta subunit of light-harvesting 1

MacromoleculeName: Beta subunit of light-harvesting 1 / type: protein_or_peptide / ID: 1 / Number of copies: 15 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 6.431528 KDa
SequenceString:
MTDKPQNDLV PDQWKPLFNN AQWLVHDIVV KTIYGGLIIA VIAHVLCWAW TPWIR

UniProtKB: Beta subunit of light-harvesting 1

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Macromolecule #2: Alpha subunit of light-harvesting 1

MacromoleculeName: Alpha subunit of light-harvesting 1 / type: protein_or_peptide / ID: 2 / Number of copies: 15 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 4.724656 KDa
SequenceString:
MKDRPFEFRT SVVVSTLLGL VMALLIHFVV LSSGAFNWLR AP

UniProtKB: Alpha subunit of light-harvesting 1

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Macromolecule #3: MULTIHEME_CYTC DOMAIN-CONTAINING PROTEIN

MacromoleculeName: MULTIHEME_CYTC DOMAIN-CONTAINING PROTEIN / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 34.923031 KDa
SequenceString: MIQQPPTLFP EITNTVRGRF YIVAGIISVV MAVASIAIFW WIFYTITPAP APPLQNPIYV NYTQEPTDYI SAESLAAMNA YIQANPQPQ AVQVLKGMTT AQISAYMVAQ VSGGLKVDCS YCHNIANFAQ QDGYPNAAKK VTARKMMLMS ADLNQNYTAK L PASVGGYQ ...String:
MIQQPPTLFP EITNTVRGRF YIVAGIISVV MAVASIAIFW WIFYTITPAP APPLQNPIYV NYTQEPTDYI SAESLAAMNA YIQANPQPQ AVQVLKGMTT AQISAYMVAQ VSGGLKVDCS YCHNIANFAQ QDGYPNAAKK VTARKMMLMS ADLNQNYTAK L PASVGGYQ ITCATCHNGK AAGLEPYPIE IMNTLPNDWR LPLELDYPGG LVVTGRKDVS NHEVEQNQFA MYHMNVSMGQ GC TFCHNAR YFPSYEIAQK NHSIIMLQMT KHIQETYVAP GGRIADGIMA GKSPSCWLCH QGANIPPGAA KPGQVPAVLS STP

UniProtKB: Uncharacterized protein

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Macromolecule #4: Reaction center protein L chain

MacromoleculeName: Reaction center protein L chain / type: protein_or_peptide / ID: 4
Details: The L- and M-subunits of the RC are encoded by a fused gene pufLM but post-translational processed into two discrete subunits each containing six and five transmembrane helices
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 34.84423 KDa
SequenceString: MSAVPRALPL PSGETLPAEA ISSTGSQAAS AEVIPFSIIE EFYKRPGKTL AARFFGVDPF DFWIGRFYVG LFGAISIIGI ILGVAFYLY EGVVNEGTLN ILAMRIEPPP VSQGLNVDPA QPGFFWFLTM VAATIAFVGW LLRQIDISLK LDMGMEVPIA F GAVVSSWI ...String:
MSAVPRALPL PSGETLPAEA ISSTGSQAAS AEVIPFSIIE EFYKRPGKTL AARFFGVDPF DFWIGRFYVG LFGAISIIGI ILGVAFYLY EGVVNEGTLN ILAMRIEPPP VSQGLNVDPA QPGFFWFLTM VAATIAFVGW LLRQIDISLK LDMGMEVPIA F GAVVSSWI TLQWLRPIAM GAWGHGFPLG ITHHLDWVSN IGYQYYNFFY NPFHAIGITL LFASTLFLHM HGSAVLSEAK RN ISDQNIH VFWRNILGYS IGEIGIHRVA FWTGAASVLF SNLCIFLSGT FVKDWNAFWG FWDKMPIWNG VGQGALVA

UniProtKB: Reaction center protein L chain

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Macromolecule #5: Reaction center protein M chain

MacromoleculeName: Reaction center protein M chain / type: protein_or_peptide / ID: 5
Details: The L- and M-subunits of the RC are encoded by a fused gene pufLM but post-translational processed into two discrete subunits each containing six and five transmembrane helices
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 35.046078 KDa
SequenceString: PIDLHDEEYR DGLEGTIAKP PGHVGWMQRL LGEGQVGPIY VGLWGVISFI TFFASAFIIL VDYGRQVGWN PIIYLREFWN LAVYPPPTE YGLSWNVPWD KGGAWLAATF FLHISVLTWW ARLYTRAKAT GVGTQLAWGF ASALSLYFVI YLFHPLALGN W SAAPGHGF ...String:
PIDLHDEEYR DGLEGTIAKP PGHVGWMQRL LGEGQVGPIY VGLWGVISFI TFFASAFIIL VDYGRQVGWN PIIYLREFWN LAVYPPPTE YGLSWNVPWD KGGAWLAATF FLHISVLTWW ARLYTRAKAT GVGTQLAWGF ASALSLYFVI YLFHPLALGN W SAAPGHGF RAILDWTNYV SIHWGNFYYN PFHMLSIFFL LGSTLLLAMH GATIVATSKW KSEMEFTEMM AEGPGTQRAQ LF WRWVMGW NANSYNIHIW AWWFAAFTAI TGAIGLFLSG TLVPDWYAWG ETAKIVAPWP NPDWAQYVFR

UniProtKB: Reaction center protein L chain

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Macromolecule #6: Subunit X

MacromoleculeName: Subunit X / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 3.628477 KDa
SequenceString:
MAPFLMAFFT IVLIVATLYF LSMIMSGKPE SR

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Macromolecule #7: Subunit Y

MacromoleculeName: Subunit Y / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 4.493262 KDa
SequenceString:
MNWIVATFML MFVLVAFLPL VVSLAYTWVT NPETQSTEE

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Macromolecule #8: Subunit Z

MacromoleculeName: Subunit Z / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Roseiflexus castenholzii DSM 13941 (bacteria)
Molecular weightTheoretical: 6.927004 KDa
SequenceString:
MDFLILLQAE PSPWPVWSGY ALCFVPLAAV ILGFIIAARF TDKQATSAYL RLDPAKANEP EQG

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Macromolecule #9: BACTERIOCHLOROPHYLL A

MacromoleculeName: BACTERIOCHLOROPHYLL A / type: ligand / ID: 9 / Number of copies: 48 / Formula: BCL
Molecular weightTheoretical: 911.504 Da
Chemical component information

ChemComp-BCL:
BACTERIOCHLOROPHYLL A / Bacteriochlorophyll

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Macromolecule #10: beta,psi-caroten-4-one

MacromoleculeName: beta,psi-caroten-4-one / type: ligand / ID: 10 / Number of copies: 30 / Formula: KGD
Molecular weightTheoretical: 550.856 Da
Chemical component information

ChemComp-KGD:
beta,psi-caroten-4-one

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Macromolecule #11: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 11 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

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Macromolecule #12: BACTERIOPHEOPHYTIN B

MacromoleculeName: BACTERIOPHEOPHYTIN B / type: ligand / ID: 12 / Number of copies: 3 / Formula: BPB
Molecular weightTheoretical: 887.199 Da
Chemical component information

ChemComp-BPB:
BACTERIOPHEOPHYTIN B / Pheophytin

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Macromolecule #13: 2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E,30E,34E,38E)-3,7,11,15,19,...

MacromoleculeName: 2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E,30E,34E,38E)-3,7,11,15,19,23,27,31,35,39,43-undecamethyltetratetraconta-2,6,10,1 4,18,22,26,30,34,38,42-undecaen-1-yl]naphthalene-1,4-dione
type: ligand / ID: 13 / Number of copies: 3 / Formula: MQE
Molecular weightTheoretical: 921.467 Da

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Macromolecule #14: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

MacromoleculeName: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE
type: ligand / ID: 14 / Number of copies: 3 / Formula: PGV
Molecular weightTheoretical: 749.007 Da
Chemical component information

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM / Phosphatidylglycerol

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Macromolecule #15: FE (III) ION

MacromoleculeName: FE (III) ION / type: ligand / ID: 15 / Number of copies: 1 / Formula: FE
Molecular weightTheoretical: 55.845 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 272617

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