1t0f

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spinqualitylabelsall models 1t0f, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the TnsA/TnsC(504-555) complex

Overview

Tn7 transposition requires the assembly of a nucleoprotein complex, containing four self-encoded proteins, transposon ends, and target DNA., Within this complex, TnsC, the molecular switch that regulates, transposition, and TnsA, one part of the transposase, interact directly., Here, we demonstrate that residues 504-555 of TnsC are responsible for, TnsA/TnsC interaction. The crystal structure of the TnsA/TnsC(504-555), complex, resolved to 1.85 A, illustrates the burial of a large hydrophobic, patch on the surface of TnsA. One consequence of sequestering this patch, is a marked increase in the thermal stability of TnsA as shown by, differential scanning calorimetry. A model based on the complex structure, suggested that TnsA and a slightly longer version of the cocrystallized, TnsC fragment (residues 495-555) might cooperate to bind DNA, a prediction, confirmed using gel mobility shift assays. Donor DNA binding by the, TnsA/TnsC(495-555) complex is correlated with the activation of the TnsAB, transposase, as measured by double-stranded DNA cleavage assays, demonstrating the importance of the TnsA/TnsC interaction in affecting Tn7, transposition.

About this Structure

1T0F is a Protein complex structure of sequences from Escherichia coli with MG, MLA and MPD as ligands. Full crystallographic information is available from OCA.

Reference

The carboxy-terminal portion of TnsC activates the Tn7 transposase through a specific interaction with TnsA., Ronning DR, Li Y, Perez ZN, Ross PD, Hickman AB, Craig NL, Dyda F, EMBO J. 2004 Aug 4;23(15):2972-81. Epub 2004 Jul 15. PMID:15257292

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