Structural highlights
Function
[DPPA_BACSU] Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacillus subtilis DppA is a binuclear zinc-dependent, D-specific aminopeptidase. The X-ray structure of the enzyme has been determined at 2.4 A resolution by a three-wavelength MAD experiment. The structure reveals that DppA is a new example of a 'self-compartmentalizing protease', a family of proteolytic complexes. Proteasomes are the most extensively studied representatives of this family. The DppA enzyme is composed of identical 30 kDa subunits organized in a decamer with 52 point-group symmetry. A 20 A wide channel runs through the complex, giving access to a central chamber holding the active sites. The structure shows DppA to be a prototype of a new family of metalloaminopeptidases characterized by the SXDXEG key sequence.
Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease.,Remaut H, Bompard-Gilles C, Goffin C, Frere JM, Van Beeumen J Nat Struct Biol. 2001 Aug;8(8):674-8. PMID:11473256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Remaut H, Bompard-Gilles C, Goffin C, Frere JM, Van Beeumen J. Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease. Nat Struct Biol. 2001 Aug;8(8):674-8. PMID:11473256 doi:10.1038/90380
