1HI9
Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.
Summary for 1HI9
| Entry DOI | 10.2210/pdb1hi9/pdb |
| Descriptor | DIPEPTIDE TRANSPORT PROTEIN DPPA, ZINC ION (3 entities in total) |
| Functional Keywords | hydrolase (protease), protease, d-aminopeptidase, decamer, self-compartmentalizing |
| Biological source | BACILLUS SUBTILIS |
| Total number of polymer chains | 5 |
| Total formula weight | 152037.44 |
| Authors | Remaut, H.,Bompard-Gilles, C.,Goffin, C.,Frere, J.M.,Van Beeumen, J. (deposition date: 2001-01-04, release date: 2001-08-09, Last modification date: 2024-05-08) |
| Primary citation | Remaut, H.,Bompard-Gilles, C.,Goffin, C.,Frere, J.M.,Van Beeumen, J. Structure of the Bacillus Subtilis D-Aminopeptidase Dppa Reveals a Novel Self-Compartmentalizing Protease Nat.Struct.Biol., 8:674-, 2001 Cited by PubMed 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. PubMed: 11473256DOI: 10.1038/90380 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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