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| | <StructureSection load='1xf6' size='340' side='right'caption='[[1xf6]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='1xf6' size='340' side='right'caption='[[1xf6]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xf6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodomonas_sp._cs24 Rhodomonas sp. cs24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XF6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xf6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodomonas_sp._CS24 Rhodomonas sp. CS24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XF6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DBV:15,16-DIHYDROBILIVERDIN'>DBV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYZ:5-HYDROXYLYSINE'>LYZ</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DBV:15,16-DIHYDROBILIVERDIN'>DBV</scene>, <scene name='pdbligand=LYZ:5-HYDROXYLYSINE'>LYZ</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qgw|1qgw]]</div></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xf6 OCA], [https://pdbe.org/1xf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1xf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xf6 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xf6 OCA], [https://pdbe.org/1xf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1xf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xf6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHE3_RHDS2 PHE3_RHDS2]] Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex. [[https://www.uniprot.org/uniprot/PHEB_RHDS2 PHEB_RHDS2]] Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex. [[https://www.uniprot.org/uniprot/PHE2_RHDS2 PHE2_RHDS2]] Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
| + | [https://www.uniprot.org/uniprot/PHE3_RHDS2 PHE3_RHDS2] Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rhodomonas sp. cs24]] | + | [[Category: Rhodomonas sp. CS24]] |
| - | [[Category: Curmi, P M.G]] | + | [[Category: Curmi PMG]] |
| - | [[Category: Doust, A B]] | + | [[Category: Doust AB]] |
| - | [[Category: Harrop, S J]] | + | [[Category: Harrop SJ]] |
| - | [[Category: Marai, C N.J]] | + | [[Category: Marai CNJ]] |
| - | [[Category: Scholes, G D]] | + | [[Category: Scholes GD]] |
| - | [[Category: Wilk, K E]] | + | [[Category: Wilk KE]] |
| - | [[Category: Cryptophyte]]
| + | |
| - | [[Category: Light-harvesting protein]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Phycoerythrin]]
| + | |
| Structural highlights
1xf6 is a 4 chain structure with sequence from Rhodomonas sp. CS24. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.1Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PHE3_RHDS2 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 PubMed
Cryptophyte algae differ from cyanobacteria and red algae in the architecture of their photosynthetic light harvesting systems, even though all three are evolutionarily related. Central to cryptophyte light harvesting is the soluble antenna protein phycoerythrin 545 (PE545). The ultrahigh resolution crystal structure of PE545, isolated from a unicellular cryptophyte Rhodomonas CS24, is reported at both 1.1A and 0.97A resolution, revealing details of the conformation and environments of the chromophores. Absorption, emission and polarized steady state spectroscopy (298K, 77K), as well as ultrafast (20fs time resolution) measurements of population dynamics are reported. Coupled with complementary quantum chemical calculations of electronic transitions of the bilins, these enable assignment of spectral absorption characteristics to each chromophore in the structure. Spectral differences between the tetrapyrrole pigments due to chemical differences between bilins, as well as their binding and interaction with the local protein environment are described. Based on these assignments, and considering customized optical properties such as strong coupling, a model for light harvesting by PE545 is developed which explains the fast, directional harvesting of excitation energy. The excitation energy is funnelled from four peripheral pigments (beta158,beta82) into a central chromophore dimer (beta50/beta61) in approximately 1ps. Those chromophores, in turn, transfer the excitation energy to the red absorbing molecules located at the periphery of the complex in approximately 4ps. A final resonance energy transfer step sensitizes just one of the alpha19 bilins on a time scale of 22ps. Furthermore, it is concluded that binding of PE545 to the thylakoid membrane is not essential for efficient energy transfer to the integral membrane chlorophyll a-containing complexes associated with PS-II.
Developing a structure-function model for the cryptophyte phycoerythrin 545 using ultrahigh resolution crystallography and ultrafast laser spectroscopy.,Doust AB, Marai CN, Harrop SJ, Wilk KE, Curmi PM, Scholes GD J Mol Biol. 2004 Nov 12;344(1):135-53. PMID:15504407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Doust AB, Marai CN, Harrop SJ, Wilk KE, Curmi PM, Scholes GD. Developing a structure-function model for the cryptophyte phycoerythrin 545 using ultrahigh resolution crystallography and ultrafast laser spectroscopy. J Mol Biol. 2004 Nov 12;344(1):135-53. PMID:15504407 doi:10.1016/j.jmb.2004.09.044
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