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| | <StructureSection load='2hez' size='340' side='right'caption='[[2hez]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2hez' size='340' side='right'caption='[[2hez]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hez]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/As_1.2186 As 1.2186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HEZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hez]] is a 2 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=2HEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HEZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hf0|2hf0]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bsh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 AS 1.2186])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Choloylglycine_hydrolase Choloylglycine hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.24 3.5.1.24] </span></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=2hez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hez OCA], [https://pdbe.org/2hez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hez RCSB], [https://www.ebi.ac.uk/pdbsum/2hez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hez ProSAT]</span></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=2hez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hez OCA], [https://pdbe.org/2hez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hez RCSB], [https://www.ebi.ac.uk/pdbsum/2hez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hez ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CBH_BIFLN CBH_BIFLN] 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 amid bond in all six major human 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). Is totally inactive toward penicillin V (PubMed:16905539).<ref>PMID:10831430</ref> <ref>PMID:16905539</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 1 2186]] | + | [[Category: Bifidobacterium longum]] |
| - | [[Category: Choloylglycine hydrolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brannigan, J A]] | + | [[Category: Brannigan JA]] |
| - | [[Category: Kumar, R S]] | + | [[Category: Kumar RS]] |
| - | [[Category: Suresh, C G]] | + | [[Category: Suresh CG]] |
| - | [[Category: Alpha]]
| + | |
| - | [[Category: Beta]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
CBH_BIFLN 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 amid bond in all six major human 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). Is totally inactive toward penicillin V (PubMed:16905539).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alphabetabetaalpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.
Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase.,Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:16905539[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tanaka H, Hashiba H, Kok J, Mierau I. Bile salt hydrolase of Bifidobacterium longum-biochemical and genetic characterization. Appl Environ Microbiol. 2000 Jun;66(6):2502-12. PMID:10831430 doi:10.1128/AEM.66.6.2502-2512.2000
- ↑ Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG. Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:16905539 doi:10.1074/jbc.M604172200
- ↑ Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG. Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:16905539 doi:10.1074/jbc.M604172200
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