1phn: Difference between revisions
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==STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION== | ==STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION== | ||
<StructureSection load='1phn' size='340' side='right' caption='[[1phn]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='1phn' size='340' side='right' caption='[[1phn]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1phn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phn OCA], [http://pdbe.org/1phn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1phn RCSB], [http://www.ebi.ac.uk/pdbsum/1phn PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1phn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phn OCA], [http://pdbe.org/1phn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1phn RCSB], [http://www.ebi.ac.uk/pdbsum/1phn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1phn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ph/1phn_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ph/1phn_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:24, 15 February 2018
STRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTIONSTRUCTURE OF PHYCOCYANIN FROM CYANIDIUM CALDARIUM AT 1.65A RESOLUTION
Structural highlights
Function[PHCA_GALSU] Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex. [PHCB_GALSU] Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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