5hpz: Difference between revisions
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The | ==type II water soluble Chl binding proteins== | ||
<StructureSection load='5hpz' size='340' side='right'caption='[[5hpz]], [[Resolution|resolution]] 1.96Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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'>[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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8H0F0_BRAOV Q8H0F0_BRAOV] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27098554</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bednarczyk | <div class="pdbe-citations 5hpz" style="background-color:#fffaf0;"></div> | ||
[[Category: Dym | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Brassicaceae]] | |||
[[Category: Large Structures]] | |||
[[Category: Bednarczyk D]] | |||
[[Category: Dym O]] | |||
[[Category: Noy D]] | |||
[[Category: Prabahard V]] | |||
Latest revision as of 10:50, 16 August 2023
type II water soluble Chl binding proteins
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