Table 1.
The amino acids constituting the secondary structures elements and the protein domains of the NEET proteins
| Protein | Cluster binding | β-Cap |
|---|---|---|
| Bact. MiNT | 1–12, 25–48, 61–79 | 13–24, 49–60 |
| At-NEET | 44–59, 74–103 | 60–73, 104–108 |
| mNT | 42–58, 72–101 | 59–71, 102–108 |
| NAF-1 | 68–84, 99–128 | 85–98, 129–135 |
| β 1 | β 2 | β 3 | β 4 | α1 | |
|---|---|---|---|---|---|
| Bact. MiNT | 13–16 | 23–24 | 49–50 | 57–60 | – |
| At-NEET | 60–63 | 70–73 | 104–107 | – | 89–96 |
| mNT | 59–62 | 68–71 | 102–105 | – | 86–94 |
| NAF-1 | 85–88 | 95–98 | 129–132 | – | 113–121 |
| Cys1 | Cys2 | Cys3 | His | |
|---|---|---|---|---|
| Bact. MiNT | 25,61 | 27,63 | 36,72 | 40,67 |
| At-NEET | 74 | 76 | 85 | 89 |
| mNT | 72 | 74 | 83 | 87 |
| NAF-1 | 99 | 101 | 110 | 114 |
The table details the amino acid indexes comprising the NEET cluster binding and β-cap domains (top panel); β-strands and α-helix of a single monomer (middle panel); and the coordinating residues of the [2Fe-2S] clusters (low panel). The Cysi indexing follow the sequence of the conserved CDGSH domain. In MiNT the values of the two CDGSH domains of the protein are indicated. One should note that the amino acids relate to the structure of different NEET proteins solved by X-ray crystallography: At-NEET, 3s2q [30]; mitoNEET, 2qh7 [15]; NAF-1, 4oo7 [38]; bacterial MiNT, 3tbn [30]