6ET5

Reaction centre light harvesting complex 1 from Blc. virids


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.87 Å
  • Aggregation State: CELL 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Cryo-EM structure of the Blastochloris viridis LH1-RC complex at 2.9 angstrom.

Qian, P.Siebert, C.A.Wang, P.Canniffe, D.P.Hunter, C.N.

(2018) Nature 556: 203-208

  • DOI: https://doi.org/10.1038/s41586-018-0014-5
  • Primary Citation of Related Structures:  
    6ET5

  • PubMed Abstract: 

    The light-harvesting 1-reaction centre (LH1-RC) complex is a key functional component of bacterial photosynthesis. Here we present a 2.9 Å resolution cryo-electron microscopy structure of the bacteriochlorophyll b-based LH1-RC complex from Blastochloris viridis that reveals the structural basis for absorption of infrared light and the molecular mechanism of quinone migration across the LH1 complex. The triple-ring LH1 complex comprises a circular array of 17 β-polypeptides sandwiched between 17 α- and 16 γ-polypeptides. Tight packing of the γ-apoproteins between β-polypeptides collectively interlocks and stabilizes the LH1 structure; this, together with the short Mg-Mg distances of bacteriochlorophyll b pairs, contributes to the large redshift of bacteriochlorophyll b absorption. The 'missing' 17th γ-polypeptide creates a pore in the LH1 ring, and an adjacent binding pocket provides a folding template for a quinone, Q P , which adopts a compact, export-ready conformation before passage through the pore and eventual diffusion to the cytochrome bc 1 complex.


  • Organizational Affiliation

    Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Photosynthetic reaction center cytochrome c subunitA [auth C]333Blastochloris viridisMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P07173 (Blastochloris viridis)
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UniProt GroupP07173
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Reaction center protein L chainB [auth L]274Blastochloris viridisMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P06009 (Blastochloris viridis)
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UniProt GroupP06009
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Reaction center protein M chainC [auth M]323Blastochloris viridisMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P06010 (Blastochloris viridis)
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Reaction center protein H chainD [auth H]258Blastochloris viridisMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P06008 (Blastochloris viridis)
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UniProt GroupP06008
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Light-harvesting protein B-1015 alpha chain59Blastochloris viridisMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P04123 (Blastochloris viridis)
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Light-harvesting protein B-1015 beta chain56Blastochloris viridisMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P04124 (Blastochloris viridis)
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
Light-harvesting protein B-1015 gamma chain24Blastochloris viridisMutation(s): 0 
UniProt
Find proteins for P04126 (Blastochloris viridis)
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UniProt GroupP04126
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Small Molecules
Ligands 10 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BCB
Query on BCB

Download Ideal Coordinates CCD File 
AC [auth 1]
BD [auth W]
CC [auth F]
DC [auth K]
DD [auth Z]
AC [auth 1],
BD [auth W],
CC [auth F],
DC [auth K],
DD [auth Z],
EC [auth P],
FC [auth S],
FD [auth c],
GB [auth L],
GC [auth V],
HB [auth L],
HC [auth Y],
HD [auth f],
IC [auth b],
JC [auth e],
JD [auth i],
KC [auth h],
LC [auth k],
LD [auth l],
MC [auth n],
NC [auth q],
ND [auth o],
OC [auth t],
PB [auth M],
PC [auth w],
PD [auth r],
QB [auth M],
QC [auth 3],
RD [auth u],
SC [auth 6],
TC [auth G],
TD [auth x],
VC [auth N],
VD [auth 4],
XC [auth Q],
XD [auth 7],
ZB [auth z],
ZC [auth T]
BACTERIOCHLOROPHYLL B
C55 H72 Mg N4 O6
QNWPCDKNPGOYNP-DSENBSCCSA-M
BPB
Query on BPB

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IB [auth L],
RB [auth M]
BACTERIOPHEOPHYTIN B
C55 H74 N4 O6
SFKCKJXMIAKQMY-GTTFDWDMSA-N
UQ9
Query on UQ9

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JB [auth L],
RC [auth 6]
Ubiquinone-9
C54 H82 O4
UUGXJSBPSRROMU-YJKFELPISA-N
MQ9
Query on MQ9

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TB [auth M]MENAQUINONE-9
C56 H80 O2
WCRXHNIUHQUASO-ABFXHILCSA-N
HEM
Query on HEM

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CB [auth C],
DB [auth C],
EB [auth C],
FB [auth C]
PROTOPORPHYRIN IX CONTAINING FE
C34 H32 Fe N4 O4
KABFMIBPWCXCRK-RGGAHWMASA-L
NS0
Query on NS0

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AD [auth T]
BC [auth 1]
CD [auth W]
ED [auth Z]
GD [auth c]
AD [auth T],
BC [auth 1],
CD [auth W],
ED [auth Z],
GD [auth c],
ID [auth f],
KD [auth i],
MD [auth l],
OD [auth o],
QD [auth r],
SD [auth u],
UC [auth G],
UD [auth x],
WC [auth N],
WD [auth 4],
YC [auth Q],
YD [auth 7]
all-trans-1,2-dihydroneurosporene
C40 H60
NHKJSVKSSGKUCH-XILUKMICSA-N
NS5
Query on NS5

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UB [auth M]15-cis-1,2-dihydroneurosporene
C40 H60
NHKJSVKSSGKUCH-DBWJSHEJSA-N
LDA
Query on LDA

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SB [auth M],
VB [auth H]
LAURYL DIMETHYLAMINE-N-OXIDE
C14 H31 N O
SYELZBGXAIXKHU-UHFFFAOYSA-N
SO4
Query on SO4

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LB [auth M]
MB [auth M]
NB [auth M]
OB [auth M]
WB [auth H]
LB [auth M],
MB [auth M],
NB [auth M],
OB [auth M],
WB [auth H],
XB [auth H],
YB [auth H]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
FE
Query on FE

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KB [auth L]FE (III) ION
Fe
VTLYFUHAOXGGBS-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
FME
Query on FME
D [auth H]L-PEPTIDE LINKINGC6 H11 N O3 SMET
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.87 Å
  • Aggregation State: CELL 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION2.0
MODEL REFINEMENTREFMAC5.7

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
European Research Council--

Revision History  (Full details and data files)

  • Version 1.0: 2018-04-11
    Type: Initial release
  • Version 1.1: 2018-04-18
    Changes: Data collection, Database references
  • Version 1.2: 2018-05-30
    Changes: Data collection, Structure summary
  • Version 1.3: 2018-10-10
    Changes: Data collection, Refinement description, Structure summary
  • Version 1.4: 2018-10-24
    Changes: Advisory, Data collection, Derived calculations, Structure summary
  • Version 1.5: 2019-10-23
    Changes: Data collection, Other