8vhs | pdb_00008vhs

X-ray Structure of a De Novo Designed Self Assembled Peptide Tetramer Featuring a Cu(His)4(H2O) Coordination Motif

spinqualitylabelsall models 8vhs, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vhs is a 4 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.36Å Ligands: ACE, CU, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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