 |
PDBsum entry 6m6c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
6m6c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
226 a.a.
|
|
|
|
|
|
|
|
|
|
|
1111 a.a.
|
|
|
|
|
|
|
|
|
|
|
1305 a.a.
|
|
|
|
|
|
|
|
|
|
|
94 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis of mfd-Dependent transcription termination.
|
|
|
Authors
|
|
J.Shi,
A.Wen,
M.Zhao,
S.Jin,
L.You,
Y.Shi,
S.Dong,
X.Hua,
Y.Zhang,
Y.Feng.
|
|
|
Ref.
|
|
Nucleic Acids Res, 2020,
48,
11762-11772.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Mfd-dependent transcription termination plays an important role in
transcription-coupled DNA repair, transcription-replication conflict resolution,
and antimicrobial resistance development. Despite extensive studies, the
molecular mechanism of Mfd-dependent transcription termination in bacteria
remains unclear, with several long-standing puzzles. How Mfd is activated by
stalled RNA polymerase (RNAP) and how activated Mfd translocates along the DNA
are unknown. Here, we report the single-particle cryo-electron microscopy
structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The
structures reveal that Mfd undergoes profound conformational changes upon
activation, contacts the RNAP β1 domain and its clamp, and pries open the RNAP
clamp. These structures provide a foundation for future studies aimed at
dissecting the precise mechanism of Mfd-dependent transcription termination and
pave the way for rational drug design targeting Mfd for the purpose of tackling
the antimicrobial resistance crisis.
|
|
|
|
|
|
|
