1HA7
STRUCTURE OF A LIGHT-HARVESTING PHYCOBILIPROTEIN, C-PHYCOCYANIN FROM SPIRULINA PLATENSIS AT 2.2A RESOLUTION
Summary for 1HA7
Entry DOI | 10.2210/pdb1ha7/pdb |
Descriptor | C-PHYCOCYANIN ALPHA CHAIN, C-PHYCOCYANIN BETA CHAIN, PHYCOCYANOBILIN, ... (4 entities in total) |
Functional Keywords | photosynthesis, cyanobacteria, light-harvesting protein, pigment protein, phycocyanobilin, chromophore |
Biological source | SPIRULINA PLATENSIS (CYANOBACTERIUM, BLUE-GREEN ALGA) More |
Cellular location | Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P72509 P72508 |
Total number of polymer chains | 24 |
Total formula weight | 450089.53 |
Authors | Padyana, A.K.,Rajashankar, K.R.,Ramakumar, S. (deposition date: 2001-03-29, release date: 2002-03-28, Last modification date: 2023-12-13) |
Primary citation | Padyana, A.K.,Bhat, V.B.,Madyastha, K.M.,Rajashankar, K.R.,Ramakumar, S. Crystal Structure of a Light-Harvesting Protein C-Phycocyanin from Spirulina Platensis Biochem.Biophys.Res.Commun., 282:893-, 2001 Cited by PubMed Abstract: 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. PubMed: 11352634DOI: 10.1006/BBRC.2001.4663 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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