1hi9

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[[Image:1hi9.gif|left|200px]]
 
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{{Structure
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==Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.==
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|PDB= 1hi9 |SIZE=350|CAPTION= <scene name='initialview01'>1hi9</scene>, resolution 2.40&Aring;
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<StructureSection load='1hi9' size='340' side='right'caption='[[1hi9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|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>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1hi9]] is a 5 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HI9 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE= DCIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi9 OCA], [https://pdbe.org/1hi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hi9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hi9 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DPPA_BACSU DPPA_BACSU] Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/1hi9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hi9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.'''
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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<ref>PMID:11473256</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1hi9" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Beeumen, J Van.]]
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[[Category: Bompard-Gilles C]]
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[[Category: Bompard-Gilles, C.]]
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[[Category: Frere JM]]
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[[Category: Frere, J M.]]
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[[Category: Goffin C]]
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[[Category: Goffin, C.]]
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[[Category: Remaut H]]
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[[Category: Remaut, H.]]
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[[Category: Van Beeumen J]]
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[[Category: d-aminopeptidase]]
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[[Category: decamer]]
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[[Category: protease]]
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[[Category: self-compartmentalizing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:31 2008''
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Current revision

Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.

PDB ID 1hi9

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