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. Author manuscript; available in PMC: 2023 Feb 18.
Published in final edited form as: Curr Opin Struct Biol. 2022 Sep 7;77:102447. doi: 10.1016/j.sbi.2022.102447

Table 1. The status of structural features identified to differ between the mammalian closed/active and open/deactive states in preparations of complex I from different species.

Species Given name PDB/EMDB Resolution (A) Reference NDUFA5/10 interface ND6 TMH3 ND3 TMH1-2 loop ND1 TMH5-6 loop ND1 TMH4 NDUFS2 β1–β2 loop NDUFS7 Arg77 loop
Mammals Bos taurus Active-apo 7QSL/14133 2.76 Chung et al. [8] Extensive A A A A A A
Deactive-apo 7QSN/14139 2.81 Chung et al. [8] Restricted D D D D D D
Mus musculus Active 6ZR2/11377 3.10 Bridges et al. [9] Extensive A A A A A A
ND6-P25L 7AK6/11811 3.82 Yin et al. [10] Restricted D D D D D D
Ovis aries Native-closed 6ZKO/11256 3.80 Kampjut et al. [11] Extensive A A A A A A
Native-open1 6ZKP/11257 3.20 Kampjut et al. [11] Restricted D D D D D D
Sus scrofa Active (CIQ) 7V2C/31640 2.90 Gu etal. [12] Extensive A A A A A A
Deactive (CIQD) 7V2D/31641 3.30 Gu etal. [12] Restricted D D D D D D
Plants Brassica oleracea Mature 7A23/11614 3.70 Soufari et al. [13] n/a D D A-like D-like Alt A-like
Arabidopsis thaliana Closed 7AR8/11876 3.53 Klusch etal. [14] n/a D D A-like D-like [Alt] Mixed
Open 7AR7/11875 3.46 Klusch etal. [14] n/a D D Alt D-like [Alt] Mixed
Single-cell eukaryotes Yarrowia lipolytica n/a 7O71/12742 2.40 Parey et al. [15] n/a D A-like A-like D A Int
Tetrahymena thermophila Closed/Active 7TGH/25882 2.60 Zhou et al. [17] n/a A A A A A A
Bacteria Thermus thermophilus n/a 6Y11/XRC 3.11 Gutierrez et al. [18] n/a D [A-like] A-like D-like Alt Mixed
Escherichia coli Conformation 1 7NYR/12653 3.90 Kolata et al. [19] n/a D D [Alt] D [Alt] [Mixed]
Thermosynechococcus vestitus NDH-1L 6HUM/0281 3.34 Schuller et al. [20] n/a D A-like A A Alt A
NDH-1MS 6TJV/10513 3.20 Schuller et al. [21] n/a D A-like A A Alt A

All the structures listed are ‘as-prepared’ enzymes that have not been treated with substrates, inhibitors or to activate or deactivate them. In S. scrofa and T. thermophila the enzyme is contained in a supercomplex. Each structural feature is compared to its structure defined in this laboratory in the ‘active’ (A) and ‘deactive’ (D) resting states of bovine complex I [8,23,35] and residue numbers are given for the bovine enzyme. Square brackets denote poor density. ND6 TMH3: A, α-helical or D, π-bulge. ND3 TMH1-2, ND1 TMH5-6 and NDUFS2 β1–β2 loops: A, matches the bovine-A loop conformation or A-like, with only minor differences; Alt, in an alternate but ordered conformation; D, disordered. ND1 TMH4: A, bent helix with Y127-Cα in the bovine-A position or A-like, bent helix with Y127-Cα towards the bovine-D position; D-like, straight helix with Y127-Cα toward the bovine-A position or D, straight helix with Y127-Ca in the bovine-D position. NDUFS7 Arg77 loop: A, Arg pointing away from NDUFS2 and an adjacent loop or A-like with the loop retracted; Mixed, state with Arg pointing away from NDUFS2 and an adjacent β-strand; D, Arg pointing towards NDUFS2 and an adjacent β-strand. Note that for A. thaliana the open and closed states correspond to the absence and presence of a domain-bridging ferredoxin supernumerary subunit, respectively, and the closed state does not have the same ordered features as the (mammalian) ‘closed’ state. Note that T. vestitus was previously known as T. elongatus. Abbreviations: n/a, not applicable; XRC, X-ray crystallography.