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The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division

View ORCID ProfileSamuel J. Craven, View ORCID ProfileSamson G.F. Condon, View ORCID ProfileGladys Diaz-Vazquez, View ORCID ProfileQiang Cui, View ORCID ProfileAlessandro Senes
doi: https://doi.org/10.1101/2021.04.21.440662
Samuel J. Craven
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
2Integrated Program in Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
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  • ORCID record for Samuel J. Craven
Samson G.F. Condon
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
2Integrated Program in Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
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  • ORCID record for Samson G.F. Condon
Gladys Diaz-Vazquez
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
3Biophysics Graduate Program, University of Wisconsin-Madison, Madison, WI 53706
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Qiang Cui
4Department of Chemistry, Boston University
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Alessandro Senes
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
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  • For correspondence: senes@wisc.edu
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Posted November 24, 2021.
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The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division
Samuel J. Craven, Samson G.F. Condon, Gladys Diaz-Vazquez, Qiang Cui, Alessandro Senes
bioRxiv 2021.04.21.440662; doi: https://doi.org/10.1101/2021.04.21.440662
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The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division
Samuel J. Craven, Samson G.F. Condon, Gladys Diaz-Vazquez, Qiang Cui, Alessandro Senes
bioRxiv 2021.04.21.440662; doi: https://doi.org/10.1101/2021.04.21.440662

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