|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5hpz' size='340' side='right'caption='[[5hpz]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='5hpz' size='340' side='right'caption='[[5hpz]], [[Resolution|resolution]] 1.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hpz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9bras 9bras]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HPZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HPZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hpz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassicaceae Brassicaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HPZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=68G:132-HYDROXYL-CHLOROPHYLL+A'>68G</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]] 1.96Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WSCP1R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3700 9BRAS])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=68G:132-HYDROXYL-CHLOROPHYLL+A'>68G</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=5hpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hpz OCA], [http://pdbe.org/5hpz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hpz RCSB], [http://www.ebi.ac.uk/pdbsum/5hpz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hpz 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=5hpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hpz OCA], [https://pdbe.org/5hpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hpz RCSB], [https://www.ebi.ac.uk/pdbsum/5hpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hpz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8H0F0_BRAOV Q8H0F0_BRAOV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Brassicaceae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bednarczyk, D]] | + | [[Category: Bednarczyk D]] |
| - | [[Category: Dym, O]] | + | [[Category: Dym O]] |
| - | [[Category: Noy, D]] | + | [[Category: Noy D]] |
| - | [[Category: Prabahard, V]] | + | [[Category: Prabahard V]] |
| - | [[Category: Chl spectra in the type ii water soluble chl binding proteins from brassicaceae]]
| + | |
| - | [[Category: Chlorophyll binding protein]]
| + | |
| Structural highlights
Function
Q8H0F0_BRAOV
Publication Abstract from PubMed
The ability to tune the light-absorption properties of chlorophylls by their protein environment is the key to the robustness and high efficiency of photosynthetic light-harvesting proteins. Unfortunately, the intricacy of the natural complexes makes it very difficult to identify and isolate specific protein-pigment interactions that underlie the spectral-tuning mechanisms. Herein we identify and demonstrate the tuning mechanism of chlorophyll spectra in type II water-soluble chlorophyll binding proteins from Brassicaceae (WSCPs). By comparing the molecular structures of two natural WSCPs we correlate a shift in the chlorophyll red absorption band with deformation of its tetrapyrrole macrocycle that is induced by changing the position of a nearby tryptophan residue. We show by a set of reciprocal point mutations that this change accounts for up to 2/3 of the observed spectral shift between the two natural variants.
Fine Tuning of Chlorophyll Spectra by Protein-Induced Ring Deformation.,Bednarczyk D, Dym O, Prabahar V, Peleg Y, Pike DH, Noy D Angew Chem Int Ed Engl. 2016 Apr 21. doi: 10.1002/anie.201512001. PMID:27098554[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bednarczyk D, Dym O, Prabahar V, Peleg Y, Pike DH, Noy D. Fine Tuning of Chlorophyll Spectra by Protein-Induced Ring Deformation. Angew Chem Int Ed Engl. 2016 Apr 21. doi: 10.1002/anie.201512001. PMID:27098554 doi:http://dx.doi.org/10.1002/anie.201512001
|
