4s2t
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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='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='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> | ||
</table> | </table> | ||
== Function == | == 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> | [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;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:25905034</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4s2t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site
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