Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae

Sergio G. Bartual, Daniel Straume, Gro Anita Stamsås, Inés G. Muñoz, Carlos Alfonso, Martín Martínez-Ripoll, Leiv Sigve Håvarstein () and Juan A. Hermoso ()
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Sergio G. Bartual: Instituto de Química-Física Rocasolano, CSIC
Daniel Straume: Biotechnology and Food Science, Norwegian University of Life Sciences
Gro Anita Stamsås: Biotechnology and Food Science, Norwegian University of Life Sciences
Inés G. Muñoz: Macromolecular Crystallography Group. Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3
Carlos Alfonso: Centro de Investigaciones Biológicas (CIB), Ramiro de Maeztu 9
Martín Martínez-Ripoll: Instituto de Química-Física Rocasolano, CSIC
Leiv Sigve Håvarstein: Biotechnology and Food Science, Norwegian University of Life Sciences
Juan A. Hermoso: Instituto de Química-Física Rocasolano, CSIC

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract Separation of daughter cells during bacterial cell division requires splitting of the septal cross wall by peptidoglycan hydrolases. In Streptococcus pneumoniae, PcsB is predicted to perform this operation. Recent evidence shows that PcsB is recruited to the septum by the transmembrane FtsEX complex, and that this complex is required for cell division. However, PcsB lacks detectable catalytic activity in vitro, and while it has been proposed that FtsEX activates PcsB, evidence for this is lacking. Here we demonstrate that PcsB has muralytic activity, and report the crystal structure of full-length PcsB. The protein adopts a dimeric structure in which the V-shaped coiled–coil (CC) domain of each monomer acts as a pair of molecular tweezers locking the catalytic domain of each dimeric partner in an inactive configuration. This suggests that the release of the catalytic domains likely requires an ATP-driven conformational change in the FtsEX complex, conveyed towards the catalytic domains through coordinated movements of the CC domain.

Date: 2014
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DOI: 10.1038/ncomms4842

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