8esi

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'''Unreleased structure'''
 
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The entry 8esi is ON HOLD until Paper Publication
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==Bile Salt Hydrolase from B. longum with covalent inhibitor bound==
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<StructureSection load='8esi' size='340' side='right'caption='[[8esi]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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Authors: Walker, M.E., Lim, L., Redinbo, M.R.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8esi]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ESI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ESI FirstGlance]. <br>
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Description: Bile Salt Hydrolase from B. longum with covalent inhibitor bound
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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]] 2.35&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=WSR:[(3~{R},5~{R},8~{R},9~{S},10~{S},13~{R},14~{S},17~{R})-17-[(2~{R})-6-fluoranyl-5-oxidanylidene-hexan-2-yl]-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1~{H}-cyclopenta[a]phenanthren-3-yl]+hydrogen+sulfate'>WSR</scene></td></tr>
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[[Category: Lim, L]]
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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=8esi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8esi OCA], [https://pdbe.org/8esi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8esi RCSB], [https://www.ebi.ac.uk/pdbsum/8esi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8esi ProSAT]</span></td></tr>
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[[Category: Walker, M.E]]
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</table>
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[[Category: Redinbo, M.R]]
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== Function ==
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[https://www.uniprot.org/uniprot/CBH_BIFLN 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]<ref>PMID:10831430</ref> <ref>PMID:16905539</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bifidobacterium longum]]
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[[Category: Large Structures]]
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[[Category: Lim L]]
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[[Category: Redinbo MR]]
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[[Category: Walker ME]]

Current revision

Bile Salt Hydrolase from B. longum with covalent inhibitor bound

PDB ID 8esi

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