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8VS5

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

8VS5 の概要
エントリーDOI10.2210/pdb8vs5/pdb
分子名称Telomere resolvase ResT (2 entities in total)
機能のキーワードtelomere resolvase, dna-binding, structural genomics, center for structural biology of infectious diseases, csbid, dna binding protein
由来する生物種Borreliella garinii
タンパク質・核酸の鎖数1
化学式量合計24219.06
構造登録者
Semper, C.,Savchenko, A.,Watanabe, N.,Center for Structural Biology of Infectious Diseases (CSBID) (登録日: 2024-01-23, 公開日: 2024-07-17, 最終更新日: 2026-08-12)
主引用文献Semper, C.,Watanabe, N.,Karimullina, E.,Patel, D.T.,Di Leo, R.,Castellanos, M.,Patel, D.H.,Chaconas, G.,Savchenko, A.
Structure analysis of the telomere resolvase from the Lyme disease spirochete Borrelia garinii reveals functional divergence of its C-terminal domain.
Nucleic Acids Res., 52:8431-8442, 2024
Cited by
PubMed Abstract: 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.
PubMed: 38979576
DOI: 10.1093/nar/gkae580
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.796 Å)
構造検証レポート
Validation report summary of 8vs5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-08-26に公開中

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