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5fpw

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==proCathepsin B S9 from Trypanosoma congolense==
==proCathepsin B S9 from Trypanosoma congolense==
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<StructureSection load='5fpw' size='340' side='right' caption='[[5fpw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='5fpw' size='340' side='right'caption='[[5fpw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fpw]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FPW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FPW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fpw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_congolense Trypanosoma congolense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FPW FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_B Cathepsin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.1 3.4.22.1] </span></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]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fpw OCA], [http://pdbe.org/5fpw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fpw RCSB], [http://www.ebi.ac.uk/pdbsum/5fpw PDBsum]</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=5fpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fpw OCA], [https://pdbe.org/5fpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fpw RCSB], [https://www.ebi.ac.uk/pdbsum/5fpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fpw 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/B2C331_TRYCO B2C331_TRYCO]
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Cysteine proteases have been shown to be essential virulence factors and drug targets in trypanosomatids and an attractive antidisease vaccine candidate for Trypanosoma congolense. Here, we describe an important amplification of genes encoding cathepsin B-like proteases unique to T. congolense. More than 13 different genes were identified, whereas only one or two highly homologous genes have been identified in other trypanosomatids. These proteases grouped into three evolutionary clusters: TcoCBc1 to TcoCBc5 and TcoCBc6, which possess the classical catalytic triad (Cys, His, and Asn), and TcoCBs7 to TcoCBs13, which contains an unusual catalytic site (Ser, Xaa, and Asn). Expression profiles showed that members of the TcoCBc1 to TcoCBc5 and the TcoCBs7 to TcoCBs13 groups are expressed mainly in bloodstream forms and localize in the lysosomal compartment. The expression of recombinant representatives of each group (TcoCB1, TcoCB6, and TcoCB12) as proenzymes showed that TcoCBc1 and TcoCBc6 are able to autocatalyze their maturation 21 and 31 residues, respectively, upstream of the predicted start of the catalytic domain. Both displayed a carboxydipeptidase function, while only TcoCBc1 behaved as an endopeptidase. TcoCBc1 exhibited biochemical differences regarding inhibitor sensitivity compared to that of other cathepsin B-like proteases. Recombinant pro-TcoCBs12 did not automature in vitro, and the pepsin-matured enzyme was inactive in tests with cathepsin B fluorogenic substrates. In vivo inhibition studies using CA074Me (a cell-permeable cathepsin B-specific inhibitor) demonstrated that TcoCB are involved in lysosomal protein degradation essential for survival in bloodstream form. Furthermore, TcoCBc1 elicited an important immune response in experimentally infected cattle. We propose this family of proteins as a potential therapeutic target and as a plausible antigen for T. congolense diagnosis.
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Molecular and biochemical characterization of a cathepsin B-like protease family unique to Trypanosoma congolense.,Mendoza-Palomares C, Biteau N, Giroud C, Coustou V, Coetzer T, Authie E, Boulange A, Baltz T Eukaryot Cell. 2008 Apr;7(4):684-97. doi: 10.1128/EC.00405-07. Epub 2008 Feb 15. PMID:18281598<ref>PMID:18281598</ref>
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==See Also==
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*[[Cathepsin 3D structures|Cathepsin 3D structures]]
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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 5fpw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cathepsin B]]
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[[Category: Large Structures]]
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[[Category: Baltz, T]]
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[[Category: Biteau, N]]
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[[Category: Franzetti, B]]
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[[Category: Sevajol, M]]
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[[Category: Vellieux, F M.D]]
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[[Category: Hydrolase]]
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[[Category: Pro cathepsin b]]
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[[Category: Trypanosoma congolense]]
[[Category: Trypanosoma congolense]]
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[[Category: Trypanosome]]
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[[Category: Baltz T]]
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[[Category: Biteau N]]
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[[Category: Franzetti B]]
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[[Category: Sevajol M]]
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[[Category: Vellieux FMD]]

Current revision

proCathepsin B S9 from Trypanosoma congolense

PDB ID 5fpw

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