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

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  • A Correction to this article was published on 01 September 2001

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 Å 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 Å 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.

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Figure 1: Structure of the DppA monomer.
Figure 2: Quaternary structure of DppA.
Figure 3: Active site organization.
Figure 4: Stereo figure showing the experimental, solvent flattened electron density map calculated using 3.1 Å MAD phases extended to 2.4 Å.

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Acknowledgements

This work was supported in part by the Belgian program on Interuniversity Poles of Attraction initiated by the Federal office for Scientific, Technical and Cultural Affaires. H.R. is a research fellow of the 'Vlaams Institut voor de Bevordering van het Wetenschappelijk-Technologisch Onderzoek in de Industrie' (IWT), and C.G. is Chercheur qualifié of the FNRS, Brussels, Belgium. We thank W.R. Rypniewski for assistance with data collection at the DESY-Hamburg outstation.

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Correspondence to Jozef Van Beeumen.

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Remaut, H., Bompard-Gilles, C., Goffin, C. et al. Structure of the Bacillus subtilis d-aminopeptidase DppA reveals a novel self-compartmentalizing protease. Nat Struct Mol Biol 8, 674–678 (2001) doi:10.1038/90380

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