6PTY
Soluble model of human CuA (Tt3Lh)
Summary for 6PTY
| Entry DOI | 10.2210/pdb6pty/pdb |
| Descriptor | Cytochrome c oxidase subunit 2, DINUCLEAR COPPER ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | cua site, electron transfer, cupredoxin fold, electron transport, oxidoreductase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 29170.72 |
| Authors | Giannini, E.,Lisa, M.N.,Morgada, M.N.,Alzari, P.M.,Vila, A.J. (deposition date: 2019-07-16, release date: 2019-11-20, Last modification date: 2023-10-11) |
| Primary citation | Morgada, M.N.,Llases, M.E.,Giannini, E.,Castro, M.A.,Alzari, P.M.,Murgida, D.H.,Lisa, M.N.,Vila, A.J. Unexpected electron spin density on the axial methionine ligand in CuAsuggests its involvement in electron pathways. Chem.Commun.(Camb.), 56:1223-1226, 2020 Cited by PubMed Abstract: The CuA center is a paradigm for the study of long-range biological electron transfer. This metal center is an essential cofactor for terminal oxidases like cytochrome c oxidase, the enzymatic complex responsible for cellular respiration in eukaryotes and in most bacteria. CuA acts as an electron hub by transferring electrons from reduced cytochrome c to the catalytic site of the enzyme where dioxygen reduction takes place. Different electron transfer pathways have been proposed involving a weak axial methionine ligand residue, conserved in all CuA sites. This hypothesis has been challenged by theoretical calculations indicating the lack of electron spin density in this ligand. Here we report an NMR study with selectively labeled methionine in a native CuA. NMR spectroscopy discloses the presence of net electron spin density in the methionine axial ligand in the two alternative ground states of this metal center. Similar spin delocalization observed on two second sphere mutants further supports this evidence. These data provide a novel view of the electronic structure of CuA centers and support previously neglected electron transfer pathways. PubMed: 31897463DOI: 10.1039/c9cc08883k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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