View source for 7wab


==Crystal structure of the prolyl endoprotease, PEP, from Aspergillus niger==
<StructureSection load='7wab' size='340' side='right'caption='[[7wab]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WAB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7wab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wab OCA], [https://pdbe.org/7wab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wab RCSB], [https://www.ebi.ac.uk/pdbsum/7wab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wab ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteases are enzymes that are not only essential for life but also industrially important. Understanding the substrate recognition mechanisms of proteases is important to enhance the use of proteases. The fungus Aspergillus produces a wide variety of proteases, including PEP, which is a prolyl endoprotease from A. niger. Although PEP exhibits amino acid sequence similarity to the serine peptidase family S28 proteins (PRCP and DPP7) that recognize Pro-X bonds in the terminal regions of peptides, PEP recognizes Pro-X bonds not only in peptides but also in proteins. To reveal the structural basis of the prolyl endoprotease activity of PEP, we determined the structure of PEP by X-ray crystallography at a resolution of 1.75 A. The PEP structure shows that PEP has a wide-open catalytic pocket compared to its homologs. The characteristic catalytic pocket structure of PEP is predicted to be important for the recognition of protein substrates.

Crystal structure and substrate recognition mechanism of the prolyl endoprotease PEP from Aspergillus niger.,Miyazono KI, Kubota K, Takahashi K, Tanokura M Biochem Biophys Res Commun. 2022 Feb 5;591:76-81. doi:, 10.1016/j.bbrc.2021.12.114. Epub 2022 Jan 1. PMID:34999257<ref>PMID:34999257</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wab" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus niger]]
[[Category: Large Structures]]
[[Category: Kubota, K]]
[[Category: Miyazono, K]]
[[Category: Takahashi, K]]
[[Category: Tanokura, M]]
[[Category: Hydrolase]]
[[Category: Protease]]