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| | ==Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site== | | ==Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site== |
| - | <StructureSection load='4s2t' size='340' side='right' caption='[[4s2t]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='4s2t' size='340' side='right'caption='[[4s2t]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4s2t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4s2t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=01B:(2S,3R)-3-AMINO-2-HYDROXY-4-PHENYLBUTANOIC+ACID'>01B</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=01B:(2S,3R)-3-AMINO-2-HYDROXY-4-PHENYLBUTANOIC+ACID'>01B</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=4s2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2t OCA], [https://pdbe.org/4s2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2t RCSB], [https://www.ebi.ac.uk/pdbsum/4s2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2t ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4s2r|4s2r]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">app-1, CELE_W03G9.4, W03G9.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4s2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2t OCA], [http://pdbe.org/4s2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s2t RCSB], [http://www.ebi.ac.uk/pdbsum/4s2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XPP_CAEEL XPP_CAEEL] Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (PubMed:11606206, PubMed:25905034). Has activity towards the flp-9 neuropeptide KPSFVRF-amide (PubMed:11606206).<ref>PMID:11606206</ref> <ref>PMID:25905034</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4s2t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4s2t" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Large Structures]] |
| - | [[Category: Isaac, R E]] | + | [[Category: Acharya KR]] |
| - | [[Category: Iyer, S]] | + | [[Category: Isaac RE]] |
| - | [[Category: La-Borde, P]] | + | [[Category: Iyer S]] |
| - | [[Category: Parsons, M R]] | + | [[Category: La-Borde P]] |
| - | [[Category: Payne, K A.P]] | + | [[Category: Parsons MR]] |
| - | [[Category: Turner, A J]] | + | [[Category: Payne KAP]] |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | [[Category: Turner AJ]] |
| - | [[Category: Metalloprotease]]
| + | |
| - | [[Category: Pitta-bread fold]]
| + | |
| - | [[Category: Zinc binding]]
| + | |
| Structural highlights
Function
XPP_CAEEL Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (PubMed:11606206, PubMed:25905034). Has activity towards the flp-9 neuropeptide KPSFVRF-amide (PubMed:11606206).[1] [2]
Publication Abstract from PubMed
Eukaryotic aminopeptidase P1 (APP1), also known as X-prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are resistant to cleavage by most peptidases. We show that recombinant and catalytically active Caenorhabditis elegans APP-1 is a dimer that uses dinuclear zinc at the active site and, for the first time, we provide structural information for a eukaryotic APP-1 in complex with the inhibitor, apstatin. Our analysis reveals that C. elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases.
Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site.,Iyer S, La-Borde PJ, Payne KA, Parsons MR, Turner AJ, Isaac RE, Acharya KR FEBS Open Bio. 2015 Apr 2;5:292-302. doi: 10.1016/j.fob.2015.03.013. eCollection , 2015. PMID:25905034[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Laurent V, Brooks DR, Coates D, Isaac RE. Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans. Eur J Biochem. 2001 Oct;268(20):5430-8. PMID:11606206 doi:10.1046/j.0014-2956.2001.02483.x
- ↑ Iyer S, La-Borde PJ, Payne KA, Parsons MR, Turner AJ, Isaac RE, Acharya KR. Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site. FEBS Open Bio. 2015 Apr 2;5:292-302. doi: 10.1016/j.fob.2015.03.013. eCollection , 2015. PMID:25905034 doi:http://dx.doi.org/10.1016/j.fob.2015.03.013
- ↑ Iyer S, La-Borde PJ, Payne KA, Parsons MR, Turner AJ, Isaac RE, Acharya KR. Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site. FEBS Open Bio. 2015 Apr 2;5:292-302. doi: 10.1016/j.fob.2015.03.013. eCollection , 2015. PMID:25905034 doi:http://dx.doi.org/10.1016/j.fob.2015.03.013
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