期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 42, 页码 11151-11156出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1711754114
关键词
type; R-M system; EcoKI; MTase; crystal structure
资金
- National Natural Science Foundation of China [31371310, 31570794, 31670903]
- Chinese Academy of Sciences Pilot Strategic Science and Technology Projects B Grants [XDB08010301, XDB08010303, XDB08020204]
- Starting-Up Funding of the Institute of Biophysics
- Thousand Young Talents Program
Type I restriction-modification (R-M) systems are multisubunit enzymes with separate DNA-recognition (S), methylation (M), and restriction (R) subunits. Despite extensive studies spanning five decades, the detailed molecular mechanisms underlying subunit assembly and conformational transition are still unclear due to the lack of high-resolution structural information. Here, we report the atomic structure of a type I MTase complex (2M+1S) bound to DNA and cofactor S-adenosyl methionine in the open form. The intermolecular interactions between M and S subunits are mediated by a four-helix bundle motif, which also determines the specificity of the interaction. Structural comparison between open and previously reported low-resolution closed structures identifies the huge conformational changes within the MTase complex. Furthermore, biochemical results show that R subunits prefer to load onto the closed form MTase. Based on our results, we proposed an updated model for the complex assembly. The work reported here provides guidelines for future applications in molecular biology.
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