Summary for clan MG

Summary Structure Literature
Clan type peptidaseM24.001 - methionyl aminopeptidase 1 (Escherichia-type) (Escherichia coli), MEROPS Accession MER0001243 (peptidase unit: 1-264); PDB accession 1MAT
HistoryPEPTIDAS.TXT (SwissProt document)
DescriptionWater nucleophile; water bound by two cobalt or manganese ions ligated by Asp, Asp, His, Glu, Glu
Contents of clanThe clan contains a single family of metalloexopeptidases, M24.
EvidenceThe 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 foldThe 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 familiesCreatinase has a similar fold (Bazan et al., 1994).
Other databases SCOP55920


Family Family Type Peptidase Structure
M24 methionyl aminopeptidase 1 ({Escherichia}-type) (Escherichia coli) Yes

Distribution of clan MG among Kingdoms of Organisms