1PHN

STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION

Summary for 1PHN

• Entry DOI: 10.2210/pdb1phn/pdb
• Descriptor: PHYCOCYANIN, PHYCOCYANOBILIN, PHYCOERYTHROBILIN, ... (5 entities in total)
• Functional Keywords: phycocyanin, phycobilisome, electron transport
• Biological source: Cyanidium caldarium; More
• Cellular location: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side: P00306 P00311
• Total number of polymer chains: 2
• Total formula weight: 37568.40

Authors

Stec, B.,Troxler, R.F.,Teeter, M.M. (deposition date: 1995-06-21, release date: 1997-09-17, Last modification date: 2024-06-05)

Primary citation

Stec, B.,Troxler, R.F.,Teeter, M.M.
Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly.
Biophys.J., 76:2912-2921, 1999

PubMed Abstract: The crystal structure of the light-harvesting protein phycocyanin from the cyanobacterium Cyanidium caldarium with novel crystal packing has been solved at 1.65-A resolution. The structure has been refined to an R value of 18.3% with excellent backbone and side-chain stereochemical parameters. In crystals of phycocyanin used in this study, the hexamers are offset rather than aligned as in other phycocyanins that have been crystallized to date. Analysis of this crystal's unique packing leads to a proposal for phycobilisome assembly in vivo and for a more prominent role for chromophore beta-155. This new role assigned to chromophore beta-155 in phycocyanin sheds light on the numerical relationships among and function of external chromophores found in phycoerythrins and phycoerythrocyanins.

PubMed: 10354419

Experimental method

X-RAY DIFFRACTION (1.65 Å)