1phn: Difference between revisions

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New page: left|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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caption="1phn, resolution 1.65&Aring;" />
caption="1phn, resolution 1.65&Aring;" />
'''STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION'''<br />
'''STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
1PHN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cyanidium_caldarium Cyanidium caldarium] with CYC and PEB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PHN OCA].  
1PHN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cyanidium_caldarium Cyanidium caldarium] with <scene name='pdbligand=CYC:'>CYC</scene> and <scene name='pdbligand=PEB:'>PEB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHN OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Stec, B.]]
[[Category: Stec, B.]]
[[Category: Teeter, M.M.]]
[[Category: Teeter, M M.]]
[[Category: Troxler, R.F.]]
[[Category: Troxler, R F.]]
[[Category: CYC]]
[[Category: CYC]]
[[Category: PEB]]
[[Category: PEB]]
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[[Category: phycocyanin]]
[[Category: phycocyanin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:49:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:56 2008''

Revision as of 15:29, 21 February 2008

File:1phn.jpg


1phn, resolution 1.65Å

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STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION

OverviewOverview

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 StructureAbout this Structure

1PHN is a Protein complex structure of sequences from Cyanidium caldarium with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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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