5noc

Solution NMR Structure of the C-terminal domain of ParB (Spo0J)

spinqualitylabelsall models 5noc Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5noc is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SP0J_BACSU Required for the initiation of sporulation and for normal chromosome segregation. Antagonizes sporulation inhibition by Soj. It probably interacts with a specific DNA site and other proteins involved in partitioning and cell division, and antagonizes Soj in response to cell cycle events related to chromosome partitioning. Publication Abstract from PubMed The ParB protein forms DNA bridging interactions around parS to condense DNA and earmark the bacterial chromosome for segregation. The molecular mechanism underlying the formation of these ParB networks is unclear. We show here that while the central DNA binding domain is essential for anchoring at parS, this interaction is not required for DNA condensation. Structural analysis of the C-terminal domain reveals a dimer with a lysine-rich surface that binds DNA non-specifically and is essential for DNA condensation in vitro. Mutation of either the dimerisation or the DNA binding interface eliminates ParB-GFP foci formation in vivo. Moreover, the free C-terminal domain can rapidly decondense ParB networks independently of its ability to bind DNA. Our work reveals a dual role for the C-terminal domain of ParB as both a DNA binding and bridging interface, and highlights the dynamic nature of ParB networks in Bacillus subtilis. The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.,Fisher GL, Pastrana CL, Higman VA, Koh A, Taylor JA, Butterer A, Craggs T, Sobott F, Murray H, Crump MP, Moreno-Herrero F, Dillingham MS Elife. 2017 Dec 15;6. doi: 10.7554/eLife.28086. PMID:29244022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA