3qj3

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<StructureSection load='3qj3' size='340' side='right'caption='[[3qj3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3qj3' size='340' side='right'caption='[[3qj3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qj3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tenmo Tenmo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QJ3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qj3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QJ3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pCAL2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7067 TENMO])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_L Cathepsin L], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qj3 OCA], [https://pdbe.org/3qj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qj3 RCSB], [https://www.ebi.ac.uk/pdbsum/3qj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qj3 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=3qj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qj3 OCA], [https://pdbe.org/3qj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qj3 RCSB], [https://www.ebi.ac.uk/pdbsum/3qj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qj3 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q69G21_TENMO Q69G21_TENMO]
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Cathepsin L-like proteinases (CAL) are major digestive proteinases in the beetle Tenebrio molitor. Procathepsin Ls 2 (pCAL2) and 3 (pCAL3) were expressed as recombinant proteins in Escherichia coli, purified and activated under acidic conditions. Immunoblot analyses of different T. molitor larval tissues demonstrated that a polyclonal antibody to pCAL3 recognized pCAL3 and cathepsin L 3 (CAL3) only in the anterior two-thirds of midgut tissue and midgut luminal contents of T. molitor larvae. Furthermore, immunocytolocalization data indicated that pCAL3 occurs in secretory vesicles and microvilli in anterior midgut. Therefore CAL3, like cathepsin L 2 (CAL2), is a digestive enzyme secreted by T. molitor anterior midgut. CAL3 hydrolyses Z-FR-MCA and Z-RR-MCA (typical cathepsin substrates), whereas CAL2 hydrolyses only Z-FR-MCA. Active site mutants (pCAL2C25S and pCAL3C26S) were constructed by replacing the catalytic cysteine with serine to prevent autocatalytic processing. Recombinant pCAL2 and pCAL3 mutants (pCAL2C25S and pCAL3C26S) were prepared, crystallized and their 3D structures determined at 1.85 and 2.1 A, respectively. While the overall structure of these enzymes is similar to other members of the papain superfamily, structural differences in the S2 subsite explain their substrate specificities. The data also supported models for CAL trafficking to lysosomes and to secretory vesicles to be discharged into midgut contents.
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The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut.,Beton D, Guzzo CR, Ribeiro AF, Farah CS, Terra WR Insect Biochem Mol Biol. 2012 May 30. PMID:22659439<ref>PMID:22659439</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qj3" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cathepsin L]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Tenmo]]
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[[Category: Tenebrio molitor]]
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[[Category: Beton, D]]
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[[Category: Beton D]]
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[[Category: Farah, C S]]
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[[Category: Farah CS]]
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[[Category: Guzzo, C R]]
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[[Category: Guzzo CR]]
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[[Category: Terra, W R]]
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[[Category: Terra WR]]
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[[Category: Hydrolase]]
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[[Category: Larval midgut]]
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[[Category: Proteinase]]
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Revision as of 11:47, 14 March 2024

Structure of digestive procathepsin L2 proteinase from Tenebrio molitor larval midgut

PDB ID 3qj3

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