1hi9
From Proteopedia
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| - | [[Image:1hi9.gif|left|200px]]<br /> | + | [[Image:1hi9.gif|left|200px]]<br /><applet load="1hi9" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hi9" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1hi9, resolution 2.40Å" /> | caption="1hi9, resolution 2.40Å" /> | ||
'''ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.'''<br /> | '''ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1HI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HI9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: self-compartmentalizing]] | [[Category: self-compartmentalizing]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:23:55 2007'' |
Revision as of 14:14, 18 December 2007
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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 ZN 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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