8vhs
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray Structure of a De Novo Designed Self Assembled Peptide Tetramer Featuring a Cu(His)4(H2O) Coordination Motif== | |
| + | <StructureSection load='8vhs' size='340' side='right'caption='[[8vhs]], [[Resolution|resolution]] 1.36Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8vhs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VHS 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]] 1.36Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=8vhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vhs OCA], [https://pdbe.org/8vhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vhs RCSB], [https://www.ebi.ac.uk/pdbsum/8vhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vhs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metalloenzymes play essential roles in biology. However, unraveling how outer-sphere interactions can be predictably controlled to influence their functions remains a significant challenge. Inspired by Cu enzymes, we demonstrate how variations in the primary, secondary, and outer coordination-sphere interactions of de novo designed artificial copper proteins (ArCuPs) within trimeric (3SCC) and tetrameric (4SCC) self-assemblies-featuring a trigonal Cu(His)(3) and a square pyramidal Cu(His)(4)(OH(2)) coordination-influence their catalytic and electron transfer properties. While 3SCC electrocatalyzes C-H oxidation, 4SCC does not. Cu(I)-3SCC reacts more rapidly with H(2)O(2) than O(2), whereas 4SCC is less active. Electron transfer, reorganization energies, and extended H(2)O-mediated hydrogen bonding patterns provide insights into the observed reactivity differences. The inactivity of 4SCC is attributed to a significant solvent reorganization energy barrier mediated by a specific His---Glu hydrogen bond. When this hydrogen bond is disrupted, the solvent reorganization energy is reduced, and C-H peroxidation activity is restored. | ||
| - | + | Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.,Prakash D, Mitra S, Sony S, Murphy M, Andi B, Ashley L, Prasad P, Chakraborty S Nat Commun. 2025 Mar 28;16(1):3048. doi: 10.1038/s41467-025-57904-5. PMID:40155633<ref>PMID:40155633</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Chakraborty | + | <div class="pdbe-citations 8vhs" style="background-color:#fffaf0;"></div> |
| - | [[Category: Mitra | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Chakraborty S]] | ||
| + | [[Category: Mitra S]] | ||
| + | [[Category: Prakash D]] | ||
| + | [[Category: Prasad P]] | ||
Current revision
X-ray Structure of a De Novo Designed Self Assembled Peptide Tetramer Featuring a Cu(His)4(H2O) Coordination Motif
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