8ete | pdb_00008ete

Bile Salt Hydrolase from B. longum with covalent inhibitor bound

spinqualitylabelsall models 8ete, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ete is a 2 chain structure with sequence from Bifidobacterium longum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: WU5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CBH_BIFLN Possesses dual functions in bile acid metabolism (By similarity). Acts as a bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids). Can hydrolyze the amide bond in all six major human conjugated bile salts, namely glycocholate (GCA), glycodeoxycholate (GDCA), glycochenodeoxycholate (GCDCA), taurocholate (TCA), taurodeoxycholate (TDCA) and taurochenodeoxycholate (TCDCA). Shows a slight preference for glycine-conjugated bile acids as substrates (PubMed:10831430, PubMed:16905539). Also acts as an amine N-acyltransferase that conjugates a wide variety of amino acids to conjugated and non-conjugated bile acids, thus producing bacterial bile acid amidates (BBAAs) - also named microbially conjugated bile acids (MCBAs) - in the gastrointestinal tract. These BBAAs may facilitate communication between the microbiota and host through the activation of human ligand-activated transcription factors (By similarity). Is totally inactive toward penicillin V (PubMed:16905539).[UniProtKB:P0DXD2]

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