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1hi9
From Proteopedia
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | DCIAA (Bacillus subtilis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.
Overview
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.
About this Structure
1HI9 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 21:05:31 2008
