Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease.

TitleStructure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease.
Publication TypeJournal Article
Year of Publication2001
AuthorsRemaut, H., C. Bompard-Gilles, C. Goffin, J. M. Frère, and J. Van Beeumen
JournalNat Struct Biol
Volume8
Issue8
Pagination674-8
Date Published2001 Aug
ISSN1072-8368
KeywordsAmino Acid Sequence, Aminopeptidases, Bacillus subtilis, Binding Sites, Crystallography, X-Ray, Metalloproteins, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, Zinc
Abstract

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.

DOI10.1038/90380
Alternate JournalNat. Struct. Biol.
PubMed ID11473256