1hi9: Difference between revisions
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Revision as of 16:31, 30 October 2007
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ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.
OverviewOverview
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 StructureAbout this Structure
1HI9 is a [Single protein] structure of sequence from [Bacillus subtilis] with ZN as [ligand]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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