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7DEG

Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism

Summary for 7DEG
Entry DOI10.2210/pdb7deg/pdb
EMDB information30657
DescriptorCytochrome c oxidase subunit I, DINUCLEAR COPPER ION, Cytochrome oxidase subunit IIa, ... (10 entities in total)
Functional Keywordselectron cryo-microscopy, heme-copper oxidase, cytochrome c oxidase dimer, aquifex aeolicus, naphthoquinone, oxidoreductase
Biological sourceAquifex aeolicus (strain VF5)
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Total number of polymer chains6
Total formula weight183295.85
Authors
Fei, S.,Hartmut, M.,Yun, Z.,Guoliang, Z.,Shuangbo, Z. (deposition date: 2020-11-04, release date: 2021-08-04)
Primary citationZhu, G.,Zeng, H.,Zhang, S.,Juli, J.,Tai, L.,Zhang, D.,Pang, X.,Zhang, Y.,Lam, S.M.,Zhu, Y.,Peng, G.,Michel, H.,Sun, F.
The Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors.
Angew.Chem.Int.Ed.Engl., 60:13323-13330, 2021
Cited by
PubMed: 33665933
DOI: 10.1002/anie.202016785
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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