4cgk

Crystal structure of the essential protein PcsB from Streptococcus pneumoniae

spinqualitylabelsall models 4cgk, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cgk is a 2 chain structure with sequence from Strp2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EDO, MG, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae.,Bartual SG, Straume D, Stamsas GA, Munoz IG, Alfonso C, Martinez-Ripoll M, Havarstein LS, Hermoso JA Nat Commun. 2014 May 8;5:3842. doi: 10.1038/ncomms4842. PMID:24804636 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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