Full-length structure of the major autolysin LytA
文献类型：期刊论文
| 作者 | Li, Q; Cheng, W; Morlot, C; Bai, XH; Jiang, YL; Wang, WJ; Roper, DI; Vernet, T; Dong, YH; Chen, YX |
| 刊名 | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
 |
| 出版日期 | 2015 |
| 卷号 | 71期号:6页码:1373-1381 |
| 关键词 | Streptococcus pneumoniae crystal structure peptidoglycan autolysin dimerization choline-binding sites |
| 英文摘要 | 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. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Crystallography |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography |
| 收录类别 | SCI |
| WOS记录号 | WOS:000355986000015 |
| 公开日期 | 2016-05-03 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/228438]  |
| 专题 | 中国科学院高能物理研究所 |
| 推荐引用方式 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. |
入库方式： OAI收割
来源：高能物理研究所
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