1hi9: Difference between revisions
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<StructureSection load='1hi9' size='340' side='right' caption='[[1hi9]], [[Resolution|resolution]] 2.40Å' scene=''> | ==Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.== | ||
<StructureSection load='1hi9' size='340' side='right'caption='[[1hi9]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hi9]] is a 5 chain structure with sequence from [ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <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'>[ | <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 == | |||
[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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/1hi9_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/1hi9_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1hi9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ABC transporter 3D structures|ABC transporter 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 30: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bompard-Gilles | [[Category: Bompard-Gilles C]] | ||
[[Category: Frere | [[Category: Frere JM]] | ||
[[Category: Goffin | [[Category: Goffin C]] | ||
[[Category: Remaut | [[Category: Remaut H]] | ||
[[Category: | [[Category: Van Beeumen J]] | ||
Latest revision as of 11:56, 9 May 2024
Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.
Structural highlights
FunctionDPPA_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacillus 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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