1hi9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Bacillus subtilis DppA is a binuclear zinc-dependent, D-specific | + | 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== | ==About this Structure== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beeumen, J | + | [[Category: Beeumen, J Van.]] |
[[Category: Bompard-Gilles, C.]] | [[Category: Bompard-Gilles, C.]] | ||
| - | [[Category: Frere, J | + | [[Category: Frere, J M.]] |
[[Category: Goffin, C.]] | [[Category: Goffin, C.]] | ||
[[Category: Remaut, H.]] | [[Category: Remaut, H.]] | ||
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[[Category: self-compartmentalizing]] | [[Category: self-compartmentalizing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:29 2008'' |
Revision as of 11:01, 21 February 2008
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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 with as ligand. Known structural/functional Sites: , , , , , , , , and . 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
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