Summary for clan MN
| Clan type peptidase | M55.001 - D-aminopeptidase DppA (Bacillus subtilis), MEROPS Accession MER0005922 (peptidase unit: 1-274); PDB accession 1HI9 |
| History | MEROPS 6.0 (30 August 2002) |
| Description | Water nucleophile; water bound by two zinc ions ligated by Asp, Glu, His, His, Glu |
| Contents of clan | Clan MN contains a D-amino acid-specific aminopeptidase. |
| Evidence | The clan contains only family M55 with its unique protein fold (see below). |
| Catalytic mechanism | (See family M55.) |
| Peptidase activity | (See family M55.) |
| Protein fold | The tertiary structure determined for the D-aminopeptidase DppA from Bacillus subtilis shows that the peptidase exists as a homodecamer organized so that the active sites are in the centre and are accessed by a channel which runs through the complex (Remaut et al., 2001). Each monomer is an alpha/beta protein with a six-strand beta sheet (in the order 321456) sandwiched between two layers of alpha helices. There is a second C-terminal domain containing a beta sheet and helices. |
| Homologous non-peptidase families | The fold is unique to clan MN. |
| Activation mechanism | (See family M55.) |
|
Other databases
| SCOP | 63992 |
Families
| M55 |
D-aminopeptidase DppA (Bacillus subtilis) |
Yes |
Distribution of clan MN among Kingdoms of Organisms
