View source for 6rnv


==The crystal structure of Thermosynechococcus elongatus protochlorophyllide oxidoreductase (POR)==
<StructureSection load='6rnv' size='340' side='right'caption='[[6rnv]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rnv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus Thermosynechococcus vestitus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RNV 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]] 1.27&#8491;</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></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=6rnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rnv OCA], [https://pdbe.org/6rnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rnv RCSB], [https://www.ebi.ac.uk/pdbsum/6rnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rnv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8DLC1_THEVB Q8DLC1_THEVB] Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).[RuleBase:RU365001]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzyme protochlorophyllide oxidoreductase (POR) catalyses a light-dependent step in chlorophyll biosynthesis that is essential to photosynthesis and, ultimately, all life on Earth(1-3). POR, which is one of three known light-dependent enzymes(4,5), catalyses reduction of the photosensitizer and substrate protochlorophyllide to form the pigment chlorophyllide. Despite its biological importance, the structural basis for POR photocatalysis has remained unknown. Here we report crystal structures of cyanobacterial PORs from Thermosynechococcus elongatus and Synechocystis sp. in their free forms, and in complex with the nicotinamide coenzyme. Our structural models and simulations of the ternary protochlorophyllide-NADPH-POR complex identify multiple interactions in the POR active site that are important for protochlorophyllide binding, photosensitization and photochemical conversion to chlorophyllide. We demonstrate the importance of active-site architecture and protochlorophyllide structure in driving POR photochemistry in experiments using POR variants and protochlorophyllide analogues. These studies reveal how the POR active site facilitates light-driven reduction of protochlorophyllide by localized hydride transfer from NADPH and long-range proton transfer along structurally defined proton-transfer pathways.

Structural basis for enzymatic photocatalysis in chlorophyll biosynthesis.,Zhang S, Heyes DJ, Feng L, Sun W, Johannissen LO, Liu H, Levy CW, Li X, Yang J, Yu X, Lin M, Hardman SJO, Hoeven R, Sakuma M, Hay S, Leys D, Rao Z, Zhou A, Cheng Q, Scrutton NS Nature. 2019 Oct 23. pii: 10.1038/s41586-019-1685-2. doi:, 10.1038/s41586-019-1685-2. PMID:31645759<ref>PMID:31645759</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rnv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermosynechococcus vestitus]]
[[Category: Levy CW]]