1hi9
From Proteopedia
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| - | [[Image:1hi9.gif|left|200px]] | + | [[Image:1hi9.gif|left|200px]] |
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| - | '''ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.''' | + | {{Structure |
| + | |PDB= 1hi9 |SIZE=350|CAPTION= <scene name='initialview01'>1hi9</scene>, resolution 2.40Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A300'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A301'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B300'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+B301'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Residue+C300'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Residue+C301'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Residue+D300'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Residue+D301'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Residue+E300'>AC9</scene> and <scene name='pdbsite=BC1:Zn+Binding+Site+For+Residue+E301'>BC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= DCIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | }} | ||
| + | |||
| + | '''ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HI9 is a [ | + | 1HI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11473256 11473256] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: self-compartmentalizing]] | [[Category: self-compartmentalizing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:28 2008'' |
Revision as of 09:37, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Sites: | , , , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | DCIAA (Bacillus subtilis) | ||||||
| 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
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