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Structural basis of DNA sequence recognition by the response regulator PhoP in Mycobacterium tuberculosis
Xiaoyuan He1, Liqin Wang1, Shuishu Wang1
1Department of Biochemistry &Molecular Biology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, Maryland 20814, USA.
Scientific Reports
|April 16, 2016
Summary
Mycobacterium tuberculosis virulence relies on the PhoP regulator. Crystal structure reveals PhoP
Area of Science:
- Molecular Biology
- Structural Biology
- Microbiology
Background:
- PhoP is an essential virulence factor in Mycobacterium tuberculosis.
- PhoP regulates virulence and is a target for anti-tuberculosis drug development.
- PhoP binds DNA as a highly cooperative dimer to direct repeats with a specific spacer.
Purpose of the Study:
- To elucidate the PhoP-DNA binding mechanism.
- To determine the crystal structure of the PhoP-DNA complex.
Main Methods:
- X-ray crystallography to determine the PhoP-DNA complex structure.
Main Results:
- Revealed a tandem PhoP dimer bound to direct repeats.
- The tandem arrangement of receiver domains formed a compact structure, explaining the 4-bp spacer requirement and cooperative binding.
- PhoP-DNA interactions involved the effector domain, with sequence-recognition helix contacting the major groove and wing interacting with the minor groove.
Conclusions:
- The crystal structure provides insights into PhoP-DNA binding mechanism.
- This structure guides the design of anti-tuberculosis drugs and vaccine strains targeting PhoP.
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