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Crystal structure of phycocyanin from heterocyst-forming filamentous cyanobacterium Nostoc sp. WR13

DOI: 10.1016/j.ijbiomac.2019.05.099 DOI Help

Authors: Hiral M. Patel (Sardar Patel University; University of Glasgow) , Aleksander W. Roszak (University of Glasgow) , Datta Madamwar (Sardar Patel University) , Richard J. Cogdell (University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: International Journal Of Biological Macromolecules

State: Published (Approved)
Published: May 2019
Diamond Proposal Number(s): 16258

Abstract: Phycocyanin (PC) is the principal pigment protein in the light-harvesting antenna of cyanobacteria. Here the biochemical characterization and the 1.51 Å crystal structure of PC from cyanobacterium Nostoc sp. WR13 (Nst-PC) is reported. The P63 crystal lattice is composed of the minimal biological entities of Nst-PC, the (αβ)3 trimeric rings. The structure has been refined to R factor 11.5% (Rfree 15.4%) using anisotropic atomic B factors. A phylogenetic study shows that the α and β chains of Nst-PC are significantly clustered in a distinct clade with Acaryochloris marina. The structure was examined to look for any significant differences between Nst-PC and PC from non-desert species. Only minor differences were found in the chromophore microenvironments. The tentative energy transfer pathways in Nst-PC were modeled based on simple structural considerations.

Journal Keywords: Crystal structure; Phycobilisome; Phycobiliproteins; Phycocyanobilin chromophore; Light harvesting complex

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)