期刊
FEBS LETTERS
卷 596, 期 16, 页码 2031-2040出版社
WILEY
DOI: 10.1002/1873-3468.14403
关键词
replicative helicase; X-ray structure
资金
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10INBS-05]
- Centre National de la Recherche Scientifique (CNRS)
- French Ministry of Education
DNA replication requires unwinding by replicative helicase. Our study discovers a new structure of bacterial helicase DnaB, which is a labile and inactive hexamer, representing an intermediate state for the active hexamer formation.
To enable chromosomal replication, DNA is unwound by the ATPase molecular motor replicative helicase. The bacterial helicase DnaB is a ring-shaped homo-hexamer whose conformational dynamics are being studied through its different 3D structural states adopted along its functional cycle. Our findings describe a new crystal structure for the apo-DnaB from Vibrio cholerae, forming a planar hexamer with pseudo-symmetry, constituted by a trimer of dimers in which the C-terminal domains delimit a triskelion-shaped hole. This hexamer is labile and inactive. We suggest that it represents an intermediate state allowing the formation of the active NTP-bound hexamer from dimers.
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