ArticleNucleic acids research2018
T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 74 citations in OpenAlex.
- Cloning and Functional Characterization of AhyAP-T65Lig, an ATP-Dependent DNA Ligase from Trabzonvirus AP-T65.Molecular biotechnology · 2026Article
- Snapshots of Motion: A Novel Structural Intermediate Reveals Conserved Dynamics in Archaeal DNA Ligases.Proteins · 2026Article
- USTAT: Unified Sequential Template Amplification and Transcription-a fully synthetic mRNA manufacturing platform.NPJ vaccines · 2026Article
- Real-Time Visualization of G2L4 Reverse Transcriptase in DNA Repair via Microhomology-Mediated End Joining.bioRxiv : the preprint server for biology · 2026Article
- Ligase-mediated programmable genomic integration (L-PGI).Nature communications · 2025Article
- Structural insights into the exchange mechanism of a replicative DNA polymerase.Nucleic acids research · 2025Article
- Structure of fungal tRNA ligase Trl1 with RNA reveals conserved substrate-binding principles.Nature structural & molecular biology · 2025Article
- Brief guide to gene cloning.Molecules and cells · 2025Review
- Crystal structure of ATP-dependent DNA ligase from Rhizobium phage vB_RleM_P10VF.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Nucleic acid joining enzymes: biological functions and synthetic applications beyond DNA.The Biochemical journal · 2025Review
- Probing the mechanism of nick searching by LIG1 at the single-molecule level.Nucleic acids research · 2024Article
- Facile Splint-Free Circularization of ssDNA with T4 DNA Ligase by Redesigning the Linear Substrate to Form an Intramolecular Dynamic Nick.Biomolecules · 2024Article
- Four Parallel Pathways in T4 Ligase-Catalyzed Repair of Nicked DNA with Diverse Bending Angles.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Characterization and genomic analysis of a lyticFrontiers in microbiology · 2024Article
- Rapid genome-wide profiling of DNA methylation and genetic variation using guide positioning sequencing (GPS).Frontiers in cell and developmental biology · 2024Article
- Engineering a Ligase Binding DNA Aptamer into a Templating DNA Scaffold to Guide the Selective Synthesis of Circular DNAzymes and DNA Aptamers.Journal of the American Chemical Society · 2023Article
- Thermostable DNA ligases from hyperthermophiles in biotechnology.Frontiers in microbiology · 2023Review
- Mismatch discrimination and sequence bias during end-joining by DNA ligases.Nucleic acids research · 2022Article
- Cryo-EM structures and biochemical insights into heterotrimeric PCNA regulation of DNA ligase.Structure (London, England : 1993) · 2022Article
- Potential application of a newly isolated phage BUCT609 infectingFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
DNA ligases play essential roles in DNA replication and repair. Bacteriophage T4 DNA ligase is the first ATP-dependent ligase enzyme to be discovered and is widely used in molecular biology, but its structure remained unknown. Our crystal structure of T4 DNA ligase bound to DNA shows a compact α-helical DNA-binding domain (DBD), nucleotidyl-transferase (NTase) domain, and OB-fold domain, which together fully encircle DNA. The DBD of T4 DNA ligase exhibits remarkable structural homology to the core DNA-binding helices of the larger DBDs from eukaryotic and archaeal DNA ligases, but it lacks additional structural components required for protein interactions. T4 DNA ligase instead has a flexible loop insertion within the NTase domain, which binds tightly to the T4 sliding clamp gp45 in a novel α-helical PIP-box conformation. Thus, T4 DNA ligase represents a prototype of the larger eukaryotic and archaeal DNA ligases, with a uniquely evolved mode of protein interaction that may be important for efficient DNA replication.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.