View source for 4bp9


==Oligopeptidase B from Trypanosoma brucei with covalently bound antipain - closed form==
<StructureSection load='4bp9' size='340' side='right'caption='[[4bp9]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bp9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomycetia Actinomycetia] and [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BP9 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]] 2.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC0:N-CARBOXY-L-PHENYLALANINE'>FC0</scene>, <scene name='pdbligand=OAR:N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE'>OAR</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=4bp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bp9 OCA], [https://pdbe.org/4bp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bp9 RCSB], [https://www.ebi.ac.uk/pdbsum/4bp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bp9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O76728_TRYBB O76728_TRYBB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oligopeptidase B cleaves after basic amino acids in peptides up to 30 residues. As a virulence factor in bacteria and trypanosomatid pathogens that is absent in higher eukaryotes, this is a promising drug target. Here we present ligand-free open state and inhibitor-bound closed state crystal structures of oligopeptidase B from Trypanosoma brucei, the causative agent of African sleeping sickness. These (and related) structures show the importance of structural dynamics, governed by a fine enthalpic and entropic balance, in substrate size selectivity and catalysis. Peptides over 30 residues cannot fit the enzyme cavity, preventing the complete domain closure required for a key propeller Asp/Glu to fix the catalytic His and Arg in the catalytically competent conformation. This size exclusion mechanism protects larger peptides and proteins from degradation. Similar bacterial prolyl endopeptidase and archael acylaminoacyl peptidase structures demonstrate this mechanism is conserved among oligopeptidase family enzymes across all three domains of life.

Crystal structures of Trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes.,Canning P, Rea D, Morty RE, Fulop V PLoS One. 2013 Nov 12;8(11):e79349. doi: 10.1371/journal.pone.0079349., eCollection 2013. PMID:24265767<ref>PMID:24265767</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bp9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinomycetia]]
[[Category: Large Structures]]
[[Category: Trypanosoma brucei]]
[[Category: Canning P]]
[[Category: Fulop V]]
[[Category: Morty R]]
[[Category: Rea D]]