7npd

Vibiro cholerae ParA2

spinqualitylabelsall models 7npd, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7npd is a 1 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KKJ2_VIBCH Publication Abstract from PubMed The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA's cooperative binding to DNA and the formation of high ParA density regions on the nucleoid. The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding.,Parker AV, Mann D, Tzokov SB, Hwang LC, Bergeron JRC Nat Commun. 2021 Aug 27;12(1):5166. doi: 10.1038/s41467-021-25429-2. PMID:34453062 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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