4CGK

Crystal structure of the essential protein PcsB from Streptococcus pneumoniae

Summary for 4CGK

• Entry DOI: 10.2210/pdb4cgk/pdb
• Descriptor: SECRETED 45 KDA PROTEIN, 1,2-ETHANEDIOL, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: cell cycle, peptidoglycan, chap, cell division
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 2
• Total formula weight: 84102.56

Authors

Bartual, S.G.,Straume, D.,Stamsas, G.A.,Alfonso, C.,Martinez-Ripoll, M.,Havarstein, L.S.,Hermoso, J.A. (deposition date: 2013-11-25, release date: 2014-05-21, Last modification date: 2024-05-08)

Primary citation

Bartual, S.G.,Straume, D.,Stamsas, G.A.,Munoz, I.G.,Alfonso, C.,Martinez-Ripoll, M.,Havarstein, L.S.,Hermoso, J.A.
Structural Basis of Pcsb-Mediated Cell Separation in Streptococcus Pneumoniae.
Nat.Commun., 5:3842-, 2014

PubMed 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.

PubMed: 24804636
DOI: 10.1038/NCOMMS4842

Experimental method

X-RAY DIFFRACTION (2.55 Å)