Title | Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease. |
Publication Type | Journal Article |
Year of Publication | 2001 |
Authors | Remaut, H., C. Bompard-Gilles, C. Goffin, J. M. Frère, and J. Van Beeumen |
Journal | Nat Struct Biol |
Volume | 8 |
Issue | 8 |
Pagination | 674-8 |
Date Published | 2001 Aug |
ISSN | 1072-8368 |
Keywords | Amino 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. |
DOI | 10.1038/90380 |
Alternate Journal | Nat. Struct. Biol. |
PubMed ID | 11473256 |
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