View source for 5hke


==bile salt hydrolase from Lactobacillus salivarius==
<StructureSection load='5hke' size='340' side='right'caption='[[5hke]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hke]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ligilactobacillus_salivarius Ligilactobacillus salivarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HKE 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]] 1.9&#8491;</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=PO4:PHOSPHATE+ION'>PO4</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=5hke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hke OCA], [https://pdbe.org/5hke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hke RCSB], [https://www.ebi.ac.uk/pdbsum/5hke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hke ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/J7H3P9_9LACO J7H3P9_9LACO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bile salt hydrolase (BSH) is a gut-bacterial enzyme that negatively influences host fat digestion and energy harvesting. The BSH enzyme activity functions as a gateway reaction in the small intestine by the deconjugation of glycine-conjugated or taurine-conjugated bile acids. Extensive gut-microbiota studies have suggested that BSH is a key mechanistic microbiome target for the development of novel non-antibiotic food additives to improve animal feed production and for the design of new measures to control obesity in humans. However, research on BSH is still in its infancy, particularly in terms of the structural basis of BSH function, which has hampered the development of BSH-based strategies for improving human and animal health. As an initial step towards the structure-function analysis of BSH, C-terminally His-tagged BSH from Lactobacillus salivarius NRRL B-30514 was crystallized in this study. The 1.90 A resolution crystal structure of L. salivarius BSH was determined by molecular replacement using the structure of Clostridium perfringens BSH as a starting model. It revealed this BSH to be a member of the N-terminal nucleophile hydrolase superfamily. Crystals of apo BSH belonged to space group P21212, with unit-cell parameters a = 90.79, b = 87.35, c = 86.76 A (PDB entry 5hke). Two BSH molecules packed perfectly as a dimer in one asymmetric unit. Comparative structural analysis of L. salivarius BSH also identified potential residues that contribute to catalysis and substrate specificity.

Crystal structure of bile salt hydrolase from Lactobacillus salivarius.,Xu F, Guo F, Hu XJ, Lin J Acta Crystallogr F Struct Biol Commun. 2016 May;72(Pt 5):376-81. doi:, 10.1107/S2053230X16005707. Epub 2016 Apr 22. PMID:27139829<ref>PMID:27139829</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hke" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Ligilactobacillus salivarius]]
[[Category: Hu X-J]]