Peptidoglycan reshaping by a noncanonical peptidase for helical cell shape in Campylobacter jejuni

Kyungjin Min, Doo Ri An, Hye-Jin Yoon, Neha Rana, Ji Su Park, Jinshil Kim, Mijoon Lee, Dusan Hesek, Sangryeol Ryu, B. Moon Kim, Shahriar Mobashery (), Se Won Suh () and Hyung Ho Lee ()
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Kyungjin Min: Seoul National University
Doo Ri An: Seoul National University
Hye-Jin Yoon: Seoul National University
Neha Rana: University of Notre Dame, Notre Dame
Ji Su Park: Seoul National University
Jinshil Kim: Seoul National University
Mijoon Lee: University of Notre Dame, Notre Dame
Dusan Hesek: University of Notre Dame, Notre Dame
Sangryeol Ryu: Seoul National University
B. Moon Kim: Seoul National University
Shahriar Mobashery: University of Notre Dame, Notre Dame
Se Won Suh: Seoul National University
Hyung Ho Lee: Seoul National University

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract Assembly of the peptidoglycan is crucial in maintaining viability of bacteria and in defining bacterial cell shapes, both of which are important for existence in the ecological niche that the organism occupies. Here, eight crystal structures for a member of the cell-shape-determining class of Campylobacter jejuni, the peptidoglycan peptidase 3 (Pgp3), are reported. Characterization of the turnover chemistry of Pgp3 reveals cell wall d,d-endopeptidase and d,d-carboxypeptidase activities. Catalysis is accompanied by large conformational changes upon peptidoglycan binding, whereby a loop regulates access to the active site. Furthermore, prior hydrolysis of the crosslinked peptide stem from the saccharide backbone of the peptidoglycan on one side is a pre-requisite for its recognition and turnover by Pgp3. These analyses reveal the noncanonical nature of the transformations at the core of the events that define the morphological shape for C. jejuni as an intestinal pathogen.

Date: 2020
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DOI: 10.1038/s41467-019-13934-4

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