1hi9

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<StructureSection load='1hi9' size='340' side='right'caption='[[1hi9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1hi9' size='340' side='right'caption='[[1hi9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1hi9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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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<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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</td></tr><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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</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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCIAA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
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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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[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<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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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>
 
==See Also==
==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Vibrio subtilis ehrenberg 1835]]
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[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[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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Revision as of 11:32, 27 March 2024

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

PDB ID 1hi9

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