5vjs
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5vjs' size='340' side='right'caption='[[5vjs]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5vjs' size='340' side='right'caption='[[5vjs]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5vjs]] is a 1 chain structure | + | <table><tr><td colspan='2'>[[5vjs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VJS FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9D7:[4-(15-phenylporphyrin-5-yl-kappa~4~N~21~,N~22~,N~23~,N~24~)benzoato(2-)]zinc'>9D7</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9D7:[4-(15-phenylporphyrin-5-yl-kappa~4~N~21~,N~22~,N~23~,N~24~)benzoato(2-)]zinc'>9D7</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5vju|5vju]], [[5vjt|5vjt]]</div></td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5vju|5vju]], [[5vjt|5vjt]]</div></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">designed ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32630 SYNTHETIC CONSTRUCT sequences])</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=5vjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vjs OCA], [https://pdbe.org/5vjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vjs RCSB], [https://www.ebi.ac.uk/pdbsum/5vjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vjs 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=5vjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vjs OCA], [https://pdbe.org/5vjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vjs RCSB], [https://www.ebi.ac.uk/pdbsum/5vjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vjs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Natural photosynthetic protein complexes capture sunlight to power the energetic catalysis that supports life on Earth. Yet these natural protein structures carry an evolutionary legacy of complexity and fragility that encumbers protein reengineering efforts and obfuscates the underlying design rules for light-driven charge separation. De novo development of a simplified photosynthetic reaction center protein can clarify practical engineering principles needed to build new enzymes for efficient solar-to-fuel energy conversion. Here, we report the rational design, X-ray crystal structure, and electron transfer activity of a multi-cofactor protein that incorporates essential elements of photosynthetic reaction centers. This highly stable, modular artificial protein framework can be reconstituted in vitro with interchangeable redox centers for nanometer-scale photochemical charge separation. Transient absorption spectroscopy demonstrates Photosystem II-like tyrosine and metal cluster oxidation, and we measure charge separation lifetimes exceeding 100 ms, ideal for light-activated catalysis. This de novo-designed reaction center builds upon engineering guidelines established for charge separation in earlier synthetic photochemical triads and modified natural proteins, and it shows how synthetic biology may lead to a new generation of genetically encoded, light-powered catalysts for solar fuel production. | ||
| + | |||
| + | De novo protein design of photochemical reaction centers.,Ennist NM, Zhao Z, Stayrook SE, Discher BM, Dutton PL, Moser CC Nat Commun. 2022 Aug 23;13(1):4937. doi: 10.1038/s41467-022-32710-5. PMID:35999239<ref>PMID:35999239</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5vjs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Synthetic construct sequences]] | ||
[[Category: Dutton, P L]] | [[Category: Dutton, P L]] | ||
[[Category: Ennist, N M]] | [[Category: Ennist, N M]] | ||
Revision as of 06:41, 31 August 2022
De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, a synthetic Zn porphyrin, and Zn(II) cations
| |||||||||||
