Structural highlights
6hrn is a 2 chain structure with sequence from Nostoc sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Ligands: | , , , , , , |
NonStd Res: | |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
Phycocyanin (PC) is the principal pigment protein in the light-harvesting antenna of cyanobacteria. Here the biochemical characterization and the 1.51A 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 (alphabeta)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 alpha and beta 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.
Crystal structure of phycocyanin from heterocyst-forming filamentous cyanobacterium Nostoc sp. WR13.,Patel HM, Roszak AW, Madamwar D, Cogdell RJ Int J Biol Macromol. 2019 May 20;135:62-68. doi: 10.1016/j.ijbiomac.2019.05.099. PMID:31121226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Patel HM, Roszak AW, Madamwar D, Cogdell RJ. Crystal structure of phycocyanin from heterocyst-forming filamentous cyanobacterium Nostoc sp. WR13. Int J Biol Macromol. 2019 May 20;135:62-68. doi: 10.1016/j.ijbiomac.2019.05.099. PMID:31121226 doi:http://dx.doi.org/10.1016/j.ijbiomac.2019.05.099