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Crystal structure of bile salt hydrolase from Lactobacillus salivarius

文献类型： 外文期刊

作者： Xu, Fuzhou 1 ; Guo, Fangfang 1 ; Hu, Xiao-Jian 2 ; Lin, Jun 3 ;

作者机构： 1.Beijing Acad Agr & Forestry Sci, Inst Anim Husb & Vet Med, Beijing Key Lab Prevent & Control Infect Dis Live, Beijing 100097, Peoples R China

2.Fudan Univ, Sch Life Sci, Dept Physiol & Biophys, Shanghai 200438, Peoples R China

3.Univ Tennessee, Dept Anim Sci, Knoxville, TN 37996 USA

关键词： bile salt hydrolase;Lactobacillus;lipid metabolism;gut microbiome;crystal structure

期刊名称：ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS （ 影响因子：1.056； 五年影响因子：1.089 ）

ISSN： 2053-230X

年卷期： 2016 年 72 卷

页码：

收录情况： SCI

摘要： 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 angstrom 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 P2(1)2(1)2, with unit-cell parameters a = 90.79, b = 87.35, c = 86.76 angstrom (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.

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