7ffp: Difference between revisions
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<StructureSection load='7ffp' size='340' side='right'caption='[[7ffp]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='7ffp' size='340' side='right'caption='[[7ffp]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7ffp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7ffp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7c9d 7c9d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FFP 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]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ffp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ffp OCA], [https://pdbe.org/7ffp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ffp RCSB], [https://www.ebi.ac.uk/pdbsum/7ffp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ffp 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=7ffp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ffp OCA], [https://pdbe.org/7ffp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ffp RCSB], [https://www.ebi.ac.uk/pdbsum/7ffp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ffp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PEPE_XENLA PEPE_XENLA] Hydrolyzes dipeptides containing N-terminal aspartate residues. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Xenopus laevis]] | ||
[[Category: | [[Category: Kumar A]] | ||
[[Category: | [[Category: Makde RD]] | ||
[[Category: | [[Category: Singh R]] | ||
Latest revision as of 20:15, 29 November 2023
Crystal structure of di-peptidase-E from Xenopus laevisCrystal structure of di-peptidase-E from Xenopus laevis
Structural highlights
FunctionPEPE_XENLA Hydrolyzes dipeptides containing N-terminal aspartate residues. Publication Abstract from PubMedGene encoding aspartyl dipeptidase from Xenopus levies (PepExl) is upregulated by thyroid hormone and is proposed to play a significant role in resorption of tadpole tail during metamorphosis. However, the importance of peptidase activity for the resorption of the tail remain elusive. Here we report the crystal structures of first eukaryotic S51 peptidase, PepExl, in its ligand-free and Asp-bound states at 1.4 and 1.8 A resolutions, respectively. The active site is located at dimeric interface and the catalytic triad is found to be dissembled in ligand-free and assembled in Asp-bound state. Structural comparison and molecular dynamic simulations of ligand-free and Asp-bound states shows that distinct loop (loop-A) plays an important role in active site shielding, substrate binding and enzyme activation. This study illuminates the Asp-X dipeptide binding in PepExl is associated with ordering of the loop-A and assembly of residues of catalytic triad in active conformation for enzymatic activity. Crystal structure of aspartyl dipeptidase from Xenopus laevis revealed ligand binding induced loop ordering and catalytic triad assembly.,Kumar A, Singh R, Ghosh B, Makde RD Proteins. 2021 Aug 25. doi: 10.1002/prot.26220. PMID:34431561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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