Structure of the peptidoglycan polymerase RodA resolved by evolutionary coupling analysis

Megan Sjodt, Kelly Brock, Genevieve Dobihal, Patricia D. A. Rohs, Anna G. Green, Thomas A. Hopf, Alexander J. Meeske, Veerasak Srisuknimit, Daniel Kahne, Suzanne Walker, Debora S. Marks, Thomas G. Bernhardt, David Z. Rudner and Andrew C. Kruse ()
Additional contact information
Megan Sjodt: Harvard Medical School
Kelly Brock: Harvard Medical School
Genevieve Dobihal: Harvard Medical School
Patricia D. A. Rohs: Harvard Medical School
Anna G. Green: Harvard Medical School
Thomas A. Hopf: Harvard Medical School
Alexander J. Meeske: Harvard Medical School
Veerasak Srisuknimit: Harvard University
Daniel Kahne: Harvard University
Suzanne Walker: Harvard Medical School
Debora S. Marks: Harvard Medical School
Thomas G. Bernhardt: Harvard Medical School
David Z. Rudner: Harvard Medical School
Andrew C. Kruse: Harvard Medical School

Nature, 2018, vol. 556, issue 7699, 118-121

Abstract: Evolutionary coupling-enabled molecular replacement determination of the structure of Thermus thermophilus RodA reveals a highly conserved cavity in its transmembrane domain, and mutagenesis experiments in Bacillus subtilis and Escherichia coli show that perturbation of this cavity abolishes RodA function.

Date: 2018
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DOI: 10.1038/nature25985

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