Summary for clan MG
| Clan type peptidase | M24.001 - methionyl aminopeptidase 1 (Escherichia-type) (Escherichia coli), MEROPS Accession MER0001243 (peptidase unit: 1-264); PDB accession 1MAT |
| History | PEPTIDAS.TXT (SwissProt document) |
| Description | Water nucleophile; water bound by two cobalt or manganese ions ligated by Asp, Asp, His, Glu, Glu |
| Contents of clan | The clan contains a single family of metalloexopeptidases, M24. |
| Evidence | The protein folds of methionyl aminopeptidase 1 (M24.001) and methionyl aminopeptidase 2 (M24.002) are unlike that of any other peptidase, and family M24 is the single family in clan MG. |
| Catalytic mechanism | (See family M24.) |
| Peptidase activity | (See family M24.) |
| Protein fold | The tertiary structure for methionyl aminopeptidase has been determined (Roderick & Matthews, 1993). Peptidases in clan M24 contain two domains derived from an ancient duplication event. Each domain contains a beta sheet and two parallel helices, and each contributes two metal ligands, which are in equivalent positions between the two domains (but are Asp in the N-terminal domain and Glu in the C-terminal domain). The N-terminal domain carries the catalytic His, and the C-terminal domain carries the fifth metal ligand, also His. |
| Evolution | (See family M24.) |
| Homologous non-peptidase families | Creatinase has a similar fold (Bazan et al., 1994). |
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Other databases
| SCOP | 55920 |
Families
| M24 |
methionyl aminopeptidase 1 ({Escherichia}-type) (Escherichia coli) |
Yes |
Distribution of clan MG among Kingdoms of Organisms
