4XB4

Structure of the N-terminal domain of OCP binding canthaxanthin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.54 Å
  • R-Value Free: 0.160 
  • R-Value Work: 0.147 
  • R-Value Observed: 0.148 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

PHOTOSYNTHESIS. A 12 angstrom carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection.

Leverenz, R.L.Sutter, M.Wilson, A.Gupta, S.Thurotte, A.Bourcier de Carbon, C.Petzold, C.J.Ralston, C.Perreau, F.Kirilovsky, D.Kerfeld, C.A.

(2015) Science 348: 1463-1466

  • DOI: https://doi.org/10.1126/science.aaa7234
  • Primary Citation of Related Structures:  
    4XB4, 4XB5

  • PubMed Abstract: 

    Pigment-protein and pigment-pigment interactions are of fundamental importance to the light-harvesting and photoprotective functions essential to oxygenic photosynthesis. The orange carotenoid protein (OCP) functions as both a sensor of light and effector of photoprotective energy dissipation in cyanobacteria. We report the atomic-resolution structure of an active form of the OCP consisting of the N-terminal domain and a single noncovalently bound carotenoid pigment. The crystal structure, combined with additional solution-state structural data, reveals that OCP photoactivation is accompanied by a 12 angstrom translocation of the pigment within the protein and a reconfiguration of carotenoid-protein interactions. Our results identify the origin of the photochromic changes in the OCP triggered by light and reveal the structural determinants required for interaction with the light-harvesting antenna during photoprotection.


  • Organizational Affiliation

    MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Orange carotenoid-binding protein
A, B
152Synechocystis sp. PCC 6803 substr. KazusaMutation(s): 0 
Gene Names: slr1963
UniProt
Find proteins for P74102 (Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa))
Explore P74102 
Go to UniProtKB:  P74102
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP74102
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.54 Å
  • R-Value Free: 0.160 
  • R-Value Work: 0.147 
  • R-Value Observed: 0.148 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 51.251α = 90
b = 64.112β = 114.89
c = 53.634γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
SCALAdata scaling
XDSdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-07-15
    Type: Initial release
  • Version 1.1: 2015-09-09
    Changes: Data collection
  • Version 1.2: 2015-12-30
    Changes: Non-polymer description
  • Version 1.3: 2017-11-22
    Changes: Derived calculations, Refinement description
  • Version 1.4: 2023-09-27
    Changes: Data collection, Database references, Refinement description