7ARC
Cryo-EM structure of Polytomella Complex-I (peripheral arm)
Summary for 7ARC
| Entry DOI | 10.2210/pdb7arc/pdb |
| EMDB information | 11879 |
| Descriptor | PSST, 13 kDa, B8, ... (23 entities in total) |
| Functional Keywords | complex-i, electron transport |
| Biological source | Polytomella sp. Pringsheim 198.80 More |
| Total number of polymer chains | 16 |
| Total formula weight | 444833.20 |
| Authors | Klusch, N.,Kuehlbrandt, W.,Yildiz, O. (deposition date: 2020-10-23, release date: 2021-12-08, Last modification date: 2024-07-10) |
| Primary citation | Klusch, N.,Senkler, J.,Yildiz, O.,Kuhlbrandt, W.,Braun, H.P. A ferredoxin bridge connects the two arms of plant mitochondrial complex I. Plant Cell, 33:2072-2091, 2021 Cited by PubMed Abstract: Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric γ-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I. PubMed: 33768254DOI: 10.1093/plcell/koab092 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.88 Å) |
Structure validation
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