Crystal structure of AimR in complex with arbitrium peptide Article Swipe
Zeyuan Guan
,
Kai Pei
,
Jing Wang
,
Yongqing Cui
,
Xiang Zhu
,
Xiang Su
,
Yuanbao Zhou
,
Delin Zhang
,
Chun Tang
,
Ping Yin
,
Zhu Liu
,
Tingting Zou
·
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.2210/pdb6jg9/pdb
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.2210/pdb6jg9/pdb
A newly identified arbitrium communication system regulates the lysis-to-lysogeny decision in a Bacillus bacteriophage. This system contains an arbitrium hexapeptide as a signal, the cellular receptor AimR, and the lysogenic negative regulator AimX. AimR specifically targets the downstream DNA to activate aimX gene expression. The arbitrium peptide binds to AimR, inhibiting its DNA-binding to promote phage lysogeny. Recently, we and other groups have elucidated how arbitrium peptide sensed by AimR. However, the molecular mechanisms of DNA recognition by AimR and the regulation of its DNA-binding activity by the peptide remain largely unknown. Here, we report the crystal structure of the AimR-DNA complex at 2.1 Å resolution. The N-terminal HTH motif recognizes the palindromic DNA sequence, buttressed by interactions between positively charged residues and the DNA phosphate groups. The DNA-bound AimR assembles a more closed dimer than the peptide-bound form. Single-molecule FRET and crosslinking assays revealed that the AimR protein samples both open and closed conformations in solution. Arbitrium peptide binding induces a closed-to-open conformational change of AimR, eliminating DNA targeting. Our structural and functional analysis provides new insights into the DNA recognition mechanism of AimR and its regulation by the arbitrium peptide in the context of phage lysis-lysogeny decisions.
Related Topics
Concepts
DNA
Lysogenic cycle
Peptide
Biology
Bacteriophage
Chemistry
Gene
Biochemistry
Molecular biology
Escherichia coli
Metadata
- Type
- paratext
- Language
- en
- Landing Page
- https://doi.org/10.2210/pdb6jg9/pdb
- OA Status
- green
- Cited By
- 11
- References
- 37
- Related Works
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- OpenAlex ID
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All OpenAlex metadata
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https://doi.org/10.2210/pdb6jg9/pdbDigital Object Identifier
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Crystal structure of AimR in complex with arbitrium peptideWork title
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paratextOpenAlex work type
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enPrimary language
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2019Year of publication
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2019-02-13Full publication date if available
- Authors
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Zeyuan Guan, Kai Pei, Jing Wang, Yongqing Cui, Xiang Zhu, Xiang Su, Yuanbao Zhou, Delin Zhang, Chun Tang, Ping Yin, Zhu Liu, Tingting ZouList of authors in order
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https://doi.org/10.2210/pdb6jg9/pdbPublisher landing page
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.ncbi.nlm.nih.gov/pmc/articles/6536502Direct OA link when available
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DNA, Lysogenic cycle, Peptide, Biology, Bacteriophage, Chemistry, Gene, Biochemistry, Molecular biology, Escherichia coliTop concepts (fields/topics) attached by OpenAlex
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