Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease.
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.
Remaut
H
H
Laboratory of Protein Biochemistry and Protein Engineering, Ghent University, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium.
Bompard-Gilles
C
C
Goffin
C
C
Frère
J M
JM
Van Beeumen
J
J
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D015032:Zinc / Q000378:metabolism
D008667:Metalloproteins; D021122:Protein Subunits; D000626:Aminopeptidases; D015032:Zinc