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Full-length structure of the major autolysin LytA
Li, Q; Cheng, W; Morlot, C; Bai, XH; Jiang, YL; Wang, WJ; Roper, DI; Vernet, T; Dong, YH; Chen, YX; Zhou, CZ; Wang WJ(王文佳); Dong YH(董宇辉)
2015
发表期刊ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
卷号71期号:6页码:1373-1381
文章类型Article
摘要LytA is responsible for the autolysis of many Streptococcus species, including pathogens such as S. pneumoniae, S. pseudopneumoniae and S. mitis. However, how this major autolysin achieves full activity remains unknown. Here, the full-length structure of the S. pneumoniae LytA dimer is reported at 2.1 angstrom resolution. Each subunit has an N-terminal amidase domain and a C-terminal choline-binding domain consisting of six choline-binding repeats, which form five canonical and one single-layered choline-binding sites. Site-directed mutageneses combined with enzymatic activity assays indicate that dimerization and binding to choline are two independent requirements for the autolytic activity of LytA in vivo. Altogether, it is suggested that dimerization and full occupancy of all choline-binding sites through binding to choline-containing TA chains enable LytA to adopt a fully active conformation which allows the amidase domain to cleave two lactyl-amide bonds located about 103 angstrom apart on the peptidoglycan.
关键词Streptococcus pneumoniae crystal structure peptidoglycan autolysin dimerization choline-binding sites
学科领域Biochemistry & Molecular Biology; Biophysics; Crystallography
DOI10.1107/S1399004715007403
收录类别SCI
WOS类目Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography
WOS记录号WOS:000355986000015
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被引频次:4[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/228438
专题多学科研究中心
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GB/T 7714
Li, Q,Cheng, W,Morlot, C,et al. Full-length structure of the major autolysin LytA[J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,2015,71(6):1373-1381.
APA Li, Q.,Cheng, W.,Morlot, C.,Bai, XH.,Jiang, YL.,...&董宇辉.(2015).Full-length structure of the major autolysin LytA.ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,71(6),1373-1381.
MLA Li, Q,et al."Full-length structure of the major autolysin LytA".ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 71.6(2015):1373-1381.
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