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| | <StructureSection load='3var' size='340' side='right'caption='[[3var]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='3var' size='340' side='right'caption='[[3var]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3var]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VAR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3var]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VAR FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vat|3vat]]</div></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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNPEP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartyl_aminopeptidase Aspartyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.21 3.4.11.21] </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=3var FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3var OCA], [https://pdbe.org/3var PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3var RCSB], [https://www.ebi.ac.uk/pdbsum/3var PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3var 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=3var FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3var OCA], [https://pdbe.org/3var PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3var RCSB], [https://www.ebi.ac.uk/pdbsum/3var PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3var ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DNPEP_BOVIN DNPEP_BOVIN]] Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism (By similarity).
| + | [https://www.uniprot.org/uniprot/DNPEP_BOVIN DNPEP_BOVIN] Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism (By similarity). |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Aminopeptidases are key enzymes involved in the regulation of signaling peptide activity. Here we present a detailed biochemical and structural analysis of an evolutionary highly conserved aspartyl aminopeptidase called DNPEP. We show that this peptidase can cleave multiple physiologically relevant substrates including angiotensins and thus may play a key role in regulating neuron function. Using a combination of X-ray crystallography, X-ray absorption spectroscopy and single particle electron microscopy analysis, we provide the first detailed structural analysis of DNPEP. We show that this enzyme possesses a binuclear Zn active site in which one of the Zn ions is readily exchangeable with other divalent cations such as Mn, which strongly stimulates the enzymatic activity of the protein. The plasticity of this metal binding site suggests a mechanism for regulation of DNPEP activity. We also demonstrate that DNPEP assembles into a functionally relevant tetrahedral complex that restricts access of peptide substrates to the active site. This structural data allows rationalization of the enzyme's preference for short peptide substrates with N-terminal acidic residues. This study provides a structural basis for understanding the physiology and bioinorganic chemistry of DNPEP and other M18 family aminopeptidases.
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| - | | + | |
| - | Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase.,Chen Y, Farquhar ER, Chance MR, Palczewski K, Kiser PD J Biol Chem. 2012 Feb 22. PMID:22356908<ref>PMID:22356908</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3var" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspartyl aminopeptidase]] | + | [[Category: Bos taurus]] |
| - | [[Category: Bovin]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y]] | + | [[Category: Chen Y]] |
| - | [[Category: Kiser, P D]] | + | [[Category: Kiser PD]] |
| - | [[Category: Palczewski, K]] | + | [[Category: Palczewski K]] |
| - | [[Category: Alpha-beta-alpha sandwich]]
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| - | [[Category: Binuclear metal center]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: M18 peptidase]]
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| - | [[Category: Mh clan]]
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| - | [[Category: Tetrahedral aminopeptidase]]
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