BIOISIS ID :: LIIIBP

Human DNA Ligase III-beta

Added: 28 September 2020

Description:

Human DNA ligase III has essential functions in nuclear and mitochondrial DNA replication and repair and contains a PARP-like zinc finger (ZnF) that increases the extent of DNA nick joining and intermolecular DNA ligation, yet the basis for ligase III specificity and structural variation among human ligases is not understood. Here combined crystal structure and small-angle X-ray scattering results reveal dynamic switching between two nick-binding components of ligase III: the ZnF-DNA binding domain (DBD) forms a crescent-shaped surface used for DNA end recognition which switches to a ring formed by the nucleotidyl transferase (NTase) and OB-fold (OBD) domains for catalysis. Structural and mutational analyses indicate that high flexibility and distinct DNA binding domain features in ligase III assist both nick sensing and the transition from nick sensing by the ZnF to nick joining by the catalytic core. The collective results support a “jackknife model” in which the ZnF loads ligase III onto nicked DNA and conformational changes deliver DNA into the active site. This work has implications for the biological specificity of DNA ligases and functions of PARP-like zinc fingers.

Total datasets deposited with submission: 1

Supporting archive file:

Download: Archive.zip

Files from original BioISIS deposit containing original dat files, models and images


Data Set:

Primary – single deposit

Description:

Batch mode experiment, collected at several concentrations. Please see publication for details

Buffer (Matrix):

50mM Tris-HCl(pH 7.5) 20.0 °C 10% glycerol, 2 mM DTT

Source: synchrotron

Instrument: ALS BL 12.3.1

Deposited files in dataset:

Download iofq_LIIIBP.dat
Loading...
Loading...
Loading...
Loading...

Real-space Transform: pofr_LIIIBP.dat dmax :: 123.0

Loading...
Download pofr_LIIIBP.dat