Global S&T Development Trend Analysis Platform of Resources and Environment
DOI | 10.1126/science.aaw4388 |
Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility | |
Reimer, Janice M.1; Eivaskhani, Maximilian1; Harb, Ingrid1; Guarne, Alba1; Weigt, Martin2; Schmeing, T. Martin1 | |
2019-11-08 | |
发表期刊 | SCIENCE |
ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2019 |
卷号 | 366期号:6466页码:706-+ |
文章类型 | Article |
语种 | 英语 |
国家 | Canada; France |
英文摘要 | Nonribosomal peptide synthetases (NRPSs) are biosynthetic enzymes that synthesize natural product therapeutics using a modular synthetic logic, whereby each module adds one aminoacyl substrate to the nascent peptide. We have determined five x-ray crystal structures of large constructs of the NRPS linear gramicidin synthetase, including a structure of a full core dimodule in conformations organized for the condensation reaction and intermodular peptidyl substrate delivery. The structures reveal differences in the relative positions of adjacent modules, which are not strictly coupled to the catalytic cycle and are consistent with small-angle x-ray scattering data. The structures and covariation analysis of homologs allowed us to create mutants that improve the yield of a peptide from a module-swapped dimodular NRPS. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000496500400041 |
WOS关键词 | SMALL-ANGLE SCATTERING ; BIOCOMBINATORIAL SYNTHESIS ; MUTATIONAL ANALYSIS ; DOMAIN ; MODULE ; BIOSYNTHESIS ; ADENYLATION ; INSIGHT ; CRYSTALLOGRAPHY ; MACROMOLECULES |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/226176 |
专题 | 环境与发展全球科技态势 |
作者单位 | 1.McGill Univ, Dept Biochem & Ctr Rech Biol Structurale, Montreal, PQ H3G 0B1, Canada; 2.Sorbonne Univ, Inst Biol Paris Seine, CNRS, Lab Computat & Quantitat Biol, F-75005 Paris, France |
推荐引用方式 GB/T 7714 | Reimer, Janice M.,Eivaskhani, Maximilian,Harb, Ingrid,et al. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility[J]. SCIENCE,2019,366(6466):706-+. |
APA | Reimer, Janice M.,Eivaskhani, Maximilian,Harb, Ingrid,Guarne, Alba,Weigt, Martin,&Schmeing, T. Martin.(2019).Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility.SCIENCE,366(6466),706-+. |
MLA | Reimer, Janice M.,et al."Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility".SCIENCE 366.6466(2019):706-+. |
条目包含的文件 | 条目无相关文件。 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论