3V3T

Crystal structure of Clostridium botulinum phage c-st TubZ

Summary for 3V3T

• Entry DOI: 10.2210/pdb3v3t/pdb
• Descriptor: Cell division GTPase FtsZ, diverged (2 entities in total)
• Functional Keywords: tubz, tubulin/ftsz related, rossmann fold, gtpase, gtp binding, structural protein
• Biological source: Clostridium botulinum C
• Total number of polymer chains: 1
• Total formula weight: 40464.11

Authors

Oliva, M.A. (deposition date: 2011-12-14, release date: 2012-05-16, Last modification date: 2024-02-28)

Primary citation

Oliva, M.A.,Martin-Galiano, A.J.,Sakaguchi, Y.,Andreu, J.M.
Tubulin homolog TubZ in a phage-encoded partition system.
Proc.Natl.Acad.Sci.USA, 109:7711-7716, 2012

PubMed Abstract: Partition systems are responsible for the process whereby large and essential plasmids are accurately positioned to daughter cells during bacterial division. They are typically made of three components: a centromere-like DNA zone, an adaptor protein, and an assembling protein that is either a Walker-box ATPase (type I) or an actin-like ATPase (type II). A recently described type III segregation system has a tubulin/FtsZ-like protein, called TubZ, for plasmid movement. Here, we present the 2.3 Å structure and dynamic assembly of a TubZ tubulin homolog from a bacteriophage and unravel the Clostridium botulinum phage c-st type III partition system. Using biochemical and biophysical approaches, we prove that a gene upstream from tubZ encodes the partner TubR and localize the centromeric region (tubS), both of which are essential for anchoring phage DNA to the motile TubZ filaments. Finally, we describe a conserved fourth component, TubY, which modulates the TubZ-R-S complex interaction.

PubMed: 22538818
DOI: 10.1073/pnas.1121546109

Experimental method

X-RAY DIFFRACTION (2.302 Å)