8v9t | pdb_00008v9t

Ecoli DnaB helicase and Phage Lambda loader P with ADP-Mg in a 6:5 stoichiometry ratio

spinqualitylabelsall models 8v9t, resolution 2.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8v9t is a 11 chain structure with sequence from Escherichia coli and Escherichia phage Lambda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.84Å Ligands: ADP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DNAB_ECOLI Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Publication Abstract from PubMed Replicative helicases need loader proteins to assemble at DNA replication origins. Multiple copies of the bacteriophage lambdaP (P) loader bind and load the Escherichia coli DnaB (B) replicative helicase onto single-stranded (ss) DNA from the replication origin. We find that the E. coli DnaB*lambdaP complex exists in two forms: B6P5 and B6P6. In the 2.66 A cryo-EM structure of B6P5, five lambdaP loader copies form a crown-like shape that tightly grips DnaB. In this complex, the closed, planar DnaB is reconfigured into an open spiral with a large enough breach to allow ssDNA to enter an internal chamber. Transition to the open spiral involves lambdaP-induced changes to the Docking Helix (DH)-Linker Helix (LH) interface. Unexpectedly, one lambdaP chain in B6P5 is positioned across the breach. The disposition of this lambdaP chain implies a complex pathway for entry of a replication-origin-derived ssDNA "bubble" ssDNA into the B6P5 complex. We propose that the B6P6 complex is an early intermediate in helicase activation in which neither DnaB nor lambdaP has reached its final form. In this complex, DnaB adopts a partially open, ajar planar configuration. lambdaP in B6P6 interacts more loosely with DnaB. The ssDNA- and ATP-binding sites in both complexes are not correctly configured for binding or hydrolysis. Our findings detail the distinct conformations of B6P6 and B6P5, allowing us to propose a structural model for the transition from an ajar planar to an open spiral configuration in the helicase loading pathway. Distinct quaternary states, intermediates, and autoinhibition during loading of the DnaB-replicative helicase by the phage lambdaP helicase loader.,Shatarupa A, Brown D, Olinares PDB, Chase J, Isiorho E, Chait BT, Jeruzalmi D Nucleic Acids Res. 2025 Nov 26;53(22):gkaf1139. doi: 10.1093/nar/gkaf1139. PMID:41312769 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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