5hpz: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
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. 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> | |||
</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> | |||
<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]</span></td></tr> | |||
</table> | |||
<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> | |||
</div> | |||
<div class="pdbe-citations 5hpz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bednarczyk, D]] | [[Category: Bednarczyk, D]] | ||
[[Category: Dym, O]] | [[Category: Dym, O]] | ||
[[Category: Noy, D]] | |||
[[Category: Prabahard, V]] | [[Category: Prabahard, V]] | ||
[[Category: | [[Category: Chl spectra in the type ii water soluble chl binding proteins from brassicaceae]] | ||
[[Category: Chlorophyll binding protein]] | |||
Revision as of 03:35, 11 May 2016
type II water soluble Chl binding proteins
| ||||||||||||
