View source for 6s2z


==Water-soluble Chlorophyll Protein (WSCP) from Brassica oleracea var. Botrytis with Chlorophyll-b==
<StructureSection load='6s2z' size='340' side='right'caption='[[6s2z]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6s2z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_oleracea_var._botrytis Brassica oleracea var. botrytis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S2Z 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]] 2.5&#8491;</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=6s2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s2z OCA], [https://pdbe.org/6s2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s2z RCSB], [https://www.ebi.ac.uk/pdbsum/6s2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s2z ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7GDB3_BRAOB Q7GDB3_BRAOB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Water-Soluble Chlorophyll Protein (WSCP) of Brassicaceae is a remarkably stable tetrapyrrole-binding protein that, by virtue of its simple design, is an exceptional model to investigate the interactions taking place between pigments and their protein scaffold and how they affect the photophysical properties and the functionality of the complexes. We investigated variants of WSCP from Lepidium virginicum (Lv) and Brassica oleracea (Bo), reconstituted with Chlorophyll (Chl) b, to determine the mechanisms by which the different Chl binding sites control their Chl a/b specificities. A combined Raman and crystallographic investigation has been employed, aimed to characterize in detail the hydrogen-bond network involving the formyl group of Chl b. The study revealed a variable degree of conformational freedom of the hydrogen bond networks among the WSCP variants, and an unexpected mixed presence of hydrogen-bonded and not hydrogen-bonded Chls b in the case of the L91P mutant of Lv WSCP. These findings helped to refine the description of the mechanisms underlying the different Chl a/b specificities of WSCP versions, highlighting the importance of the structural rigidity of the Chl binding site in the vicinity of the Chl b formyl group in granting a strong selectivity to binding sites.

How water-mediated hydrogen bonds affect chlorophyll a/b selectivity in Water-Soluble Chlorophyll Protein.,Agostini A, Meneghin E, Gewehr L, Pedron D, Palm DM, Carbonera D, Paulsen H, Jaenicke E, Collini E Sci Rep. 2019 Dec 3;9(1):18255. doi: 10.1038/s41598-019-54520-4. PMID:31796824<ref>PMID:31796824</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6s2z" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brassica oleracea var. botrytis]]
[[Category: Large Structures]]
[[Category: Agostini A]]
[[Category: Carbonera D]]
[[Category: Collini E]]
[[Category: Gewehr L]]
[[Category: Jaenicke E]]
[[Category: Meneghin E]]
[[Category: Palm DM]]
[[Category: Paulsen H]]
[[Category: Pedron D]]