1hi9

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|PDB= 1hi9 |SIZE=350|CAPTION= <scene name='initialview01'>1hi9</scene>, resolution 2.40&Aring;
|PDB= 1hi9 |SIZE=350|CAPTION= <scene name='initialview01'>1hi9</scene>, resolution 2.40&Aring;
|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>
|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>
+
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= DCIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|GENE= DCIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi9 OCA], [http://www.ebi.ac.uk/pdbsum/1hi9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hi9 RCSB]</span>
}}
}}
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[[Category: Goffin, C.]]
[[Category: Goffin, C.]]
[[Category: Remaut, H.]]
[[Category: Remaut, H.]]
-
[[Category: ZN]]
 
[[Category: d-aminopeptidase]]
[[Category: d-aminopeptidase]]
[[Category: decamer]]
[[Category: decamer]]
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[[Category: self-compartmentalizing]]
[[Category: self-compartmentalizing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:31 2008''

Revision as of 18:05, 30 March 2008


PDB ID 1hi9

Drag the structure with the mouse to rotate
, 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

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