Summary for clan MN

Summary Alignment Structure Literature
Clan type peptidaseM55.001 - D-aminopeptidase DppA (Bacillus subtilis), MEROPS Accession MER0005922 (peptidase unit: 1-274); PDB accession 1HI9
HistoryMEROPS 6.0 (30 August 2002)
DescriptionWater nucleophile; water bound by two zinc ions ligated by Asp, Glu, His, His, Glu
Contents of clanClan MN contains a D-amino acid-specific aminopeptidase.
EvidenceThe clan contains only family M55 with its unique protein fold (see below).
Catalytic mechanism(See family M55.)
Peptidase activity(See family M55.)
Protein foldThe 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 familiesThe fold is unique to clan MN.
Activation mechanism(See family M55.)
Other databases SCOP63992


Family Family Type Peptidase Structure
M55 D-aminopeptidase DppA (Bacillus subtilis) Yes

Distribution of clan MN among Kingdoms of Organisms