| Autor: |
Cargemel, Claire, Walbott, Hélène, Durand, Dominique, Legrand, Pierre, Ouldali, Malika, Ferat, Jean‐Luc, Marsin, Stéphanie, Quevillon‐Cheruel, Sophie |
| Předmět: |
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| Zdroj: |
FEBS Letters; Aug2022, Vol. 596 Issue 16, p2031-2040, 10p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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