View source for 6nag


==X-ray structure of a secreted C11 cysteine protease from Bacteroides thetaiotaomicron "iotapain==
<StructureSection load='6nag' size='340' side='right'caption='[[6nag]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nag]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NAG 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]] 2.683&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</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=6nag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nag OCA], [https://pdbe.org/6nag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nag RCSB], [https://www.ebi.ac.uk/pdbsum/6nag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nag ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8A9T8_BACTN Q8A9T8_BACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Commensal bacteria secrete proteins and metabolites to influence host intestinal homeostasis, and proteases represent a significant constituent of the components at the host:microbiome interface. Here, we determined the structures of the two secreted C11 cysteine proteases encoded by the established gut commensal Bacteroides thetaiotaomicron. We employed mutational analysis to demonstrate the two proteases, termed "thetapain" and "iotapain", undergo in trans autoactivation after lysine and/or arginine residues, as observed for other C11 proteases. We determined the structures of the active forms of thetapain and iotapain in complex with irreversible peptide inhibitors, Ac-VLTK-AOMK and biotin-VLTK-AOMK, respectively. Structural comparisons revealed key active-site interactions important for peptide recognition are more extensive for thetapain; however, both proteases employ a glutamate residue to preferentially bind small polar residues at the P2 position. Our results will aid in the design of protease-specific probes to ultimately understand the biological role of C11 proteases in bacterial fitness, elucidate their host and/or microbial substrates, and interrogate their involvement in microbiome-related diseases.

X-ray Structures of Two Bacteroides thetaiotaomicron C11 Proteases in Complex with Peptide-Based Inhibitors.,Roncase EJ, Gonzalez-Paez GE, Wolan DW Biochemistry. 2019 Apr 2;58(13):1728-1737. doi: 10.1021/acs.biochem.9b00098. Epub, 2019 Mar 14. PMID:30835452<ref>PMID:30835452</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nag" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides thetaiotaomicron VPI-5482]]
[[Category: Large Structures]]
[[Category: Gonzalez-Paez GE]]
[[Category: Roncase EJ]]
[[Category: Wolan DW]]