The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution
- Division of Molecular Biosciences, Imperial College, Exhibition Road, London SW7 2AZ (United Kingdom)
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.
- OSTI ID:
- 22360458
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, 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); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Proteomic Insights into Phycobilisome Degradation, A Selective and Tightly Controlled Process in The Fast-Growing Cyanobacterium Synechococcus elongatus UTEX 2973
The structure of allophycocyanin B from Synechocystis PCC 6803 reveals the structural basis for the extreme redshift of the terminal emitter in phycobilisomes