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• W2056523203 abstract "Significance During growth and division, bacterial cells partition the cell wall to daughter cells, but the “inside-out” signals that regulate peptidoglycan (PG) hydrolysis are not well understood. Our studies of mycobacterial proteins achieve in vitro reconstitution of the regulation of the PG hydrolase, RipC, by the FtsX extracellular domain (ECD), a ubiquitous transmembrane component of the divisome. RipC control is remarkable for the enormous conformational change encompassing the N- and C-terminal domains. The FtsX–ECD crystal structure shows not only the RipC binding site—which we confirm in vitro and in vivo—but also the flexibility of the site that provides a potential basis to control RipC affinity. Our results expand and sharpen the FtsX paradigm for regulation of PG hydrolysis." @default.
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• W2056523203 date "2014-05-19" @default.
• W2056523203 modified "2023-10-11" @default.
• W2056523203 title "<i>Mycobacterium tuberculosis</i> FtsX extracellular domain activates the peptidoglycan hydrolase, RipC" @default.
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• W2056523203 doi "https://doi.org/10.1073/pnas.1321812111" @default.
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