2X20

Structure of Peridinin-Chlorophyll-Protein reconstituted with Chl-b

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.196 
  • R-Value Work: 0.155 
  • R-Value Observed: 0.157 

Starting Model: experimental
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This is version 1.6 of the entry. See complete history. 


Literature

X-Ray Structures of the Peridinin-Chlorophyll-Protein Reconstituted with Different Chlorophylls.

Schulte, T., Hiller, R.G., Hofmann, E.

(2010) FEBS Lett 584: 973

  • DOI: https://doi.org/10.1016/j.febslet.2010.01.041
  • Primary Citation of Related Structures:  
    2X1Z, 2X20, 2X21

  • PubMed Abstract: 

    The peridinin-chlorophyll a-protein (PCP) from dinoflagellates is a soluble light harvesting antenna which gathers incoming photons mainly by the carotenoid peridinin. In PCPs reconstituted with different chlorophylls, the peridinin to chlorophyll energy transfer rates are well predicted by a Förster-like theory, but only if the pigment arrangements are identical in all PCPs. We have determined the X-ray structures of PCPs reconstituted with Chlorophyll-b (Chl-b), Chlorophyll-d (Chl-d) and Bacteriochlorophyll-a (BChl-a) to resolutions

    • Organizational Affiliation: 

    Biophysics, Department of Biology and Biotechnology, Ruhr-University Bochum, D-44780 Bochum, Germany.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PERIDININ-CHLOROPHYLL A-BINDING PROTEIN, CHLOROPLASTICA [auth M]151Amphidinium carteraeMutation(s): 0 
UniProt
Find proteins for P80484 (Amphidinium carterae)
Explore P80484 
Go to UniProtKB:  P80484
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80484
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 8 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DGD
Query on DGD
Download Ideal Coordinates CCD File 
G [auth M]DIGALACTOSYL DIACYL GLYCEROL (DGDG)
C51 H96 O15
LDQFLSUQYHBXSX-HXXRYREZSA-N
CHL
Query on CHL
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B [auth M]CHLOROPHYLL B
C55 H70 Mg N4 O6
MWVCRINOIIOUAU-UYSPMESUSA-M
PID
Query on PID
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C [auth M],
D [auth M],
E [auth M],
F [auth M]		PERIDININ
C39 H50 O7
UYRDHEJRPVSJFM-FROCQLDGSA-N
CD
Query on CD
Download Ideal Coordinates CCD File 
H [auth M]
I [auth M]
J [auth M]
K [auth M]
L [auth M]
H [auth M],
I [auth M],
J [auth M],
K [auth M],
L [auth M],
M
CADMIUM ION
Cd
WLZRMCYVCSSEQC-UHFFFAOYSA-N
PEG
Query on PEG
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S [auth M]DI(HYDROXYETHYL)ETHER
C4 H10 O3
MTHSVFCYNBDYFN-UHFFFAOYSA-N
K
Query on K
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Q [auth M]POTASSIUM ION
K
NPYPAHLBTDXSSS-UHFFFAOYSA-N
CL
Query on CL
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N [auth M],
O [auth M],
P [auth M]		CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
NA
Query on NA
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R [auth M]SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.196 
  • R-Value Work: 0.155 
  • R-Value Observed: 0.157 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 68.57α = 90
b = 82β = 90
c = 75.41γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-09
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-01-30
    Changes: Data collection, Experimental preparation, Other
  • Version 1.4: 2019-02-06
    Changes: Data collection, Experimental preparation
  • Version 1.5: 2019-04-24
    Changes: Data collection
  • Version 1.6: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description