1GH0

CRYSTAL STRUCTURE OF C-PHYCOCYANIN FROM SPIRULINA PLATENSIS

Summary for 1GH0

• Entry DOI: 10.2210/pdb1gh0/pdb
• Descriptor: C-PHYCOCYANIN ALPHA SUBUNIT, C-PHYCOCYANIN BETA SUBUNIT, PHYCOCYANOBILIN, ... (4 entities in total)
• Functional Keywords: c-phycocyanin from spirulina platensis, photosynthesis
• Biological source: Arthrospira platensis; More
• Cellular location: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P72509 P72508
• Total number of polymer chains: 24
• Total formula weight: 449489.06

Authors

Liang, D.-C.,Chang, W.-R.,Wang, X.-Q. (deposition date: 2000-10-29, release date: 2001-06-06, Last modification date: 2023-12-27)

Primary citation

Wang, X.Q.,Li, L.N.,Chang, W.R.,Zhang, J.P.,Gui, L.L.,Guo, B.J.,Liang, D.C.
Structure of C-phycocyanin from Spirulina platensis at 2.2 A resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes.
Acta Crystallogr.,Sect.D, 57:784-792, 2001

PubMed Abstract: The crystal structure of C-phycocyanin from the cyanobacterium S. platensis has been determined at 2.2 A resolution. The crystals belong to the monoclinic crystal form, which has not been previously reported for phycobiliprotein structures. The structure was solved using the molecular-replacement method with a final R value of 18.9% (R(free) = 23.7%) after model building and refinement. In the crystals used for the study, the C-phycocyanin hexamers formed by face-to-face association of two trimers are arranged in layers rather than in columns. Three different kinds of packing between adjacent hexamers in the layer were compared. The tight packing of two adjacent hexamers formed by four trimers in the asymmetric unit brings beta155 PCB chromophores close together, so it is possible that lateral energy transfer takes place through the beta155-beta155 route.

PubMed: 11375497
DOI: 10.1107/S0907444901004528

Experimental method

X-RAY DIFFRACTION (2.2 Å)