6n9j | pdb_00006n9j

X-ray structure of a secreted C11 cysteine protease from Bacteroides thetaiotaomicron in complex with an irreversible peptide inhibitor

spinqualitylabelsall models 6n9j, resolution 2.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6n9j is a 4 chain structure with sequence from Bacteroides thetaiotaomicron VPI-5482 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.17Å Ligands: ACE, CKC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8A866_BACTN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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