1ha7

Publication Abstract from PubMed

The crystal structure of C-phycocyanin, a light-harvesting phycobiliprotein from cyanobacteria (blue-green algae) Spirulina platensis has been solved by molecular replacement technique. The crystals belong to space group P2(1) with cell parameters a = 107.20, b = 115.40, c = 183.04 A; beta = 90.2 degrees. The structure has been refined to a crystallographic R factor of 19.2% (R(free) = 23.9%) using the X-ray diffraction data extending up to 2.2 A resolution. The asymmetric unit of the crystal cell consists of two (alphabeta)6-hexamers, each hexamer being the functional unit in the native antenna rod of cyanobacteria. The molecular structure resembles that of other reported C-phycocyanins. However, the unique form of aggregation of two (alphabeta)6-hexamers in the crystal asymmetric unit, suggests additional pathways of energy transfer in lateral direction between the adjacent hexamers involving beta155 phycocyanobilin chromophores.

Crystal structure of a light-harvesting protein C-phycocyanin from Spirulina platensis.,Padyana AK, Bhat VB, Madyastha KM, Rajashankar KR, Ramakumar S Biochem Biophys Res Commun. 2001 Apr 13;282(4):893-8. PMID:11352634^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.