TL;DR
The optimization of NMR experimental condition and NMR resonance assignments for the complex formed by the C-terminal DNA-binding domain of MucR and 3A3T-DNA provide a good basis for further structural study of the DNA binding and recognition mechanism of MucR.
The backbone resonance assignments of a BARD1 IDR construct spanning residues 124–270 are reported, providing a foundation for future studies aimed at understanding how the disordered regions of BARD1 interact with various binding partners, and cooperates with itself and BRCA1 to regulate genome stability.
The backbone resonance assignments of a BRCA1 IDR construct spanning residues 467–696 are reported, providing a foundation for future studies aimed at understanding how the disordered central region of BRCA1 contributes to homologous recombination, interactions with BARD1, and overall BRCA1 tumor suppressor function.
The 1H, 13C, and 15N resonance assignments of the Amblyomin-X Kunitz domain obtained by multidimensional NMR spectroscopy provide the first detailed NMR characterization of the Amblyomin-X Kunitz domain l.
In bacteria, DnaB replicative helicases are essential for unwinding genomic DNA to provide the single‐stranded templates required for replication. The recruitment of the hexameric DnaB helicase to the origin of replication is mediated by distinct mechanisms that rely on specialized factors known as helicase loaders. Th...
The symbiotic nitrogen-fixing bacterium Bradyrhizobium japonicum possess a two component regulatory system comprising FixL, a histidine kinase with O2-sensor, and FixJ, a response regulator controlling the expression of nitrogen fixation-related genes. The phosphotransfer from FixL to the N-terminal receiver domain (RE...
Escherichia coli topoisomerase III (EcTopo3) is a type IA topoisomerase that binds single-stranded DNA (ssDNA) during DNA cleavage and strand passage. Here, we report five crystal structures of EcTopo3 in complex with distinct 8-base ssDNA oligonucleotides at 1.85–2.22 Å resolution. These structures reveal a previously...
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