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1HA7

STRUCTURE OF A LIGHT-HARVESTING PHYCOBILIPROTEIN, C-PHYCOCYANIN FROM SPIRULINA PLATENSIS AT 2.2A RESOLUTION

Summary for 1HA7
Entry DOI10.2210/pdb1ha7/pdb
DescriptorC-PHYCOCYANIN ALPHA CHAIN, C-PHYCOCYANIN BETA CHAIN, PHYCOCYANOBILIN, ... (4 entities in total)
Functional Keywordsphotosynthesis, cyanobacteria, light-harvesting protein, pigment protein, phycocyanobilin, chromophore
Biological sourceSPIRULINA PLATENSIS (CYANOBACTERIUM, BLUE-GREEN ALGA)
More
Cellular locationCellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P72509 P72508
Total number of polymer chains24
Total formula weight450089.53
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 citationPadyana, 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: 11352634
DOI: 10.1006/BBRC.2001.4663
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

226707

數據於2024-10-30公開中

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