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Title: The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution

Abstract

The crystal structure of a light-harvesting protein that interacts with photosystem II is reported. Cyanobacteria and red algae use light-harvesting pigments bound by proteins to capture solar radiation and to channel excitation energy into their reaction centres. In most cyanobacteria, a multi-megadalton soluble structure known as the phycobilisome is a major light-harvesting system. Allophycocyanin is the main component of the phycobilisome core, forming a link between the rest of the phycobilisome and the reaction-centre core. The crystal structure of allophycocyanin from Thermosynechococcus elongatus (TeAPC) has been determined and refined at 3.5 Å resolution to a crystallographic R value of 26.0% (R{sub free} = 28.5%). The structure was solved by molecular replacement using the allophycocyanin structure from Spirulina platensis as the search model. The asymmetric unit contains an (αβ) monomer which is expanded by symmetry to a crystallographic trimer.

Authors:
; ;  [1]
  1. Division of Molecular Biosciences, Imperial College, Exhibition Road, London SW7 2AZ (United Kingdom)
Publication Date:
OSTI Identifier:
22360458
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 63; Journal Issue: Pt 12; Other Information: PMCID: PMC2344114; PMID: 18084078; PUBLISHER-ID: wd5086; OAI: oai:pubmedcentral.nih.gov:2344114; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CAPTURE; CRYSTAL STRUCTURE; EXCITATION; HARVESTING; MONOMERS; PHOTOSYNTHESIS; PROTEINS; RESOLUTION; SYMMETRY; VISIBLE RADIATION

Citation Formats

Murray, James William, Maghlaoui, Karim, and Barber, James. The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107050920.
Murray, James William, Maghlaoui, Karim, & Barber, James. The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution. United Kingdom. https://doi.org/10.1107/S1744309107050920
Murray, James William, Maghlaoui, Karim, and Barber, James. 2007. "The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution". United Kingdom. https://doi.org/10.1107/S1744309107050920.
@article{osti_22360458,
title = {The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution},
author = {Murray, James William and Maghlaoui, Karim and Barber, James},
abstractNote = {The crystal structure of a light-harvesting protein that interacts with photosystem II is reported. Cyanobacteria and red algae use light-harvesting pigments bound by proteins to capture solar radiation and to channel excitation energy into their reaction centres. In most cyanobacteria, a multi-megadalton soluble structure known as the phycobilisome is a major light-harvesting system. Allophycocyanin is the main component of the phycobilisome core, forming a link between the rest of the phycobilisome and the reaction-centre core. The crystal structure of allophycocyanin from Thermosynechococcus elongatus (TeAPC) has been determined and refined at 3.5 Å resolution to a crystallographic R value of 26.0% (R{sub free} = 28.5%). The structure was solved by molecular replacement using the allophycocyanin structure from Spirulina platensis as the search model. The asymmetric unit contains an (αβ) monomer which is expanded by symmetry to a crystallographic trimer.},
doi = {10.1107/S1744309107050920},
url = {https://www.osti.gov/biblio/22360458}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 12,
volume = 63,
place = {United Kingdom},
year = {Sat Dec 01 00:00:00 EST 2007},
month = {Sat Dec 01 00:00:00 EST 2007}
}