7c9b: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7c9b is ON HOLD  until Paper Publication
+==Crystal structure of dipeptidase-E from Xenopus laevis==
+<StructureSection load='7c9b' size='340' side='right'caption='[[7c9b]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7c9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C9B FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7c9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c9b OCA], [https://pdbe.org/7c9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c9b RCSB], [https://www.ebi.ac.uk/pdbsum/7c9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c9b ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PEPE_XENLA PEPE_XENLA] Hydrolyzes dipeptides containing N-terminal aspartate residues.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Gene 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.
-Authors: Kumar, A., Singh, R., Makde, R.D.
+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<ref>PMID:34431561</ref>
-Description: Crystal structure of di-peptidase-E from Xenopus laevis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Singh, R]]
+<div class="pdbe-citations 7c9b" style="background-color:#fffaf0;"></div>
-[[Category: Makde, R.D]]
+== References ==
-[[Category: Kumar, A]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Xenopus laevis]]
+[[Category: Kumar A]]
+[[Category: Makde RD]]
+[[Category: Singh R]]