Review Article
Metal Preferences of Zinc-Binding Motif on Metalloproteases
Table 1
The zinc coordination residues and the residues that fix the coordination with hydrogen bonds.
| Zinc metalloprotease | Coordination residues | Residues that form the hydrogen bond with the coordination residues | PDB no. |
| (1) Thermolysin type | (HExxH- aan-E) | α-helix-aan-α-helix | | Thermolysin | His142, His146 Glu166 | Asp170-2.8 Å-His142 Asn165-2.8 Å-His146 | 1KEI | Vibriolysin | His345, His349 Glu369 | Asp373-2.8 Å-His345 Asn368-2.8 Å-His349 | 3NQX | Staphylococcus aureus metalloproteinase | His144, His148 Glu168 | Asn167-2.8 Å-His148 Asp172-2.8 Å-His144 | 1BQB | Zinc aminopeptidase | His265, His269 Glu288 | Phe272(C=O)-2.9 Å-His269 | 1Z1W | Leukotriene A4 hydrolase | His295, His299 Glu318 | Glu325-2.8 Å-His295 Gly303(C=O)-2.6 Å-His299 | 1SQM | Human thimet oligopeptidase | His473, His477 Glu502 | Glu509-2.6 Å-His473 | 1SQM | Human neutral endopeptidase (Neprilysin) | His583, His587 Glu646 | Asp650-2.9 Å-His583 Asp590-2.7 Å-His587 | 1DMT |
| (2) Endopeptidase type | | (HExxH-aan-E or D) α-helix-aan-random coil | | Peptidyl-Lys metalloendopeptidase | His117, His121 Asp130 | Asp154-2.7 Å-His117 Thr128(C=O)-2.8 Å-His121 | 1GE6 |
| (3) Carboxypeptidase A type | | β-sheet-aan-random coil | | Carboxypeptidase A | His69, His196 Glu72 | Asp142-2.7 Å-His69 | 1YME | Putative lysostaphin peptidase | His232, His311 Asp236 | Glu315-2.6 Å-His311 Gly216(C=O)-2.8 Å-His232 | 2GU1 |
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