1phn
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(New page: 200px<br /><applet load="1phn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1phn, resolution 1.65Å" /> '''STRUCTURE OF PHYCOCY...)
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Revision as of 21:42, 20 November 2007
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STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION
Overview
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.
About this Structure
1PHN is a Protein complex structure of sequences from Cyanidium caldarium with CYC and PEB as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly., Stec B, Troxler RF, Teeter MM, Biophys J. 1999 Jun;76(6):2912-21. PMID:10354419
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