6HRN

C-Phycocyanin from heterocyst forming filamentous cyanobacterium Nostoc sp. WR13

Summary for 6HRN

• Entry DOI: 10.2210/pdb6hrn/pdb
• Descriptor: Alpha Subunit of Cyanobacterial Phycocyanin protein, Beta Subunit of Cyanobacterial Phycocyanin protein, PHYCOCYANOBILIN, ... (10 entities in total)
• Functional Keywords: photosynthesis, heterocyst forming filamentous cyanobacterium, phycobilisomes, phycocyanin, cyc chromophores
• Biological source: Nostoc sp.; More
• Total number of polymer chains: 2
• Total formula weight: 38881.79

Authors

Patel, H.M.,Roszak, A.W.,Madamwar, D.,Cogdell, R.J. (deposition date: 2018-09-27, release date: 2019-06-05, Last modification date: 2024-05-01)

Primary citation

Patel, H.M.,Roszak, A.W.,Madamwar, D.,Cogdell, R.J.
Crystal structure of phycocyanin from heterocyst-forming filamentous cyanobacterium Nostoc sp. WR13.
Int.J.Biol.Macromol., 135:62-68, 2019

PubMed 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 P6 crystal lattice is composed of the minimal biological entities of Nst-PC, the (αβ) trimeric rings. The structure has been refined to R factor 11.5% (R 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.

PubMed: 31121226
DOI: 10.1016/j.ijbiomac.2019.05.099

Experimental method

X-RAY DIFFRACTION (1.513 Å)