2l8v
From Proteopedia
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==Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A== | ==Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A== | ||
- | <StructureSection load='2l8v' size='340' side='right' caption='[[2l8v | + | <StructureSection load='2l8v' size='340' side='right'caption='[[2l8v]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2l8v]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2l8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L8V FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8v OCA], [https://pdbe.org/2l8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l8v RCSB], [https://www.ebi.ac.uk/pdbsum/2l8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8v ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/PYR1_THEVB PYR1_THEVB] Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Acton | + | [[Category: Thermosynechococcus vestitus BP-1]] |
- | [[Category: Ciccosanti | + | [[Category: Acton TB]] |
- | [[Category: Cort | + | [[Category: Ciccosanti C]] |
- | [[Category: Everett | + | [[Category: Cort JR]] |
- | [[Category: Hamilton | + | [[Category: Everett JK]] |
- | [[Category: Kennedy | + | [[Category: Hamilton K]] |
- | [[Category: Lee | + | [[Category: Kennedy MA]] |
- | [[Category: Montelione | + | [[Category: Lee D]] |
- | + | [[Category: Montelione GT]] | |
- | [[Category: Ramelot | + | [[Category: Ramelot TA]] |
- | [[Category: Xiao | + | [[Category: Xiao R]] |
- | [[Category: Yang | + | [[Category: Yang Y]] |
- | + | ||
- | + |
Current revision
Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A
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