8vs5

Structure of catalytic domain of telomere resolvase, ResT, from Borrelia garinii

spinqualitylabelsall models 8vs5, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vs5 is a 1 chain structure with sequence from Borreliella garinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.796Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B8F151_BORGR Publication Abstract from PubMed Borrelia spirochetes are the causative agents of Lyme disease and relapsing fever, two of the most common tick-borne illnesses. A characteristic feature of these spirochetes is their highly segmented genomes which consists of a linear chromosome and a mixture of up to approximately 24 linear and circular extrachromosomal plasmids. The complexity of this genomic arrangement requires multiple strategies for efficient replication and partitioning during cell division, including the generation of hairpin ends found on linear replicons mediated by the essential enzyme ResT, a telomere resolvase. Using an integrative structural biology approach employing advanced modelling, circular dichroism, X-ray crystallography and small-angle X-ray scattering, we have generated high resolution structural data on ResT from B. garinii. Our data provides the first high-resolution structures of ResT from Borrelia spirochetes and revealed active site positioning in the catalytic domain. We also demonstrate that the C-terminal domain of ResT is required for both transesterification steps of telomere resolution, and is a requirement for DNA binding, distinguishing ResT from other telomere resolvases from phage and bacteria. These results advance our understanding of the molecular function of this essential enzyme involved in genome maintenance in Borrelia pathogens. Structure analysis of the telomere resolvase from the Lyme disease spirochete Borrelia garinii reveals functional divergence of its C-terminal domain.,Semper C, Watanabe N, Karimullina E, Patel DT, Di Leo R, Castellanos M, Patel DH, Chaconas G, Savchenko A Nucleic Acids Res. 2024 Jul 9:gkae580. doi: 10.1093/nar/gkae580. PMID:38979576 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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