ArticleNucleic acids research2017
Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 23 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Bacteriophage T4 genome packaging: mechanism and application.EcoSal Plus · 2025Review
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- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- A viral genome packaging ring-ATPase is a flexibly coordinated pentamer.Nature communications · 2021Article
- Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.Nucleic acids research · 2021Article
- Function of a viral genome packaging motor from bacteriophage T4 is insensitive to DNA sequence.Nucleic acids research · 2020Article
- Recognition of an α-helical hairpin in P22 large terminase by a synthetic antibody fragment.Acta crystallographica. Section D, Structural biology · 2020Article
- Architecture of the herpesvirus genome-packaging complex and implications for DNA translocation.Protein & cell · 2020Article
- Full-length human cytomegalovirus terminase pUL89 adopts a two-domain structure specific for DNA packaging.PLoS pathogens · 2019Article
- Functional Dissection of a Viral DNA Packaging Machine's Walker B Motif.Journal of molecular biology · 2019Article
- Controlling the Revolving and Rotating Motion Direction of Asymmetric Hexameric Nanomotor by Arginine Finger and Channel Chirality.ACS nano · 2019Review
- Evidence that a catalytic glutamate and an 'Arginine Toggle' act in concert to mediate ATP hydrolysis and mechanochemical coupling in a viral DNA packaging motor.Nucleic acids research · 2019Article
- Bacteriophage N4 large terminase: expression, purification and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The crystal structure of the large terminase from the Geobacillus stearothermophilus bacteriophage D6E shows a unique relative orientation of the N-terminal adenosine triphosphatase (ATPase) and C-terminal nuclease domains. This monomeric 'initiation' state with the two domains 'locked' together is stabilized via a conserved C-terminal arm, which may interact with the portal protein during motor assembly, as predicted for several bacteriophages. Further work supports the formation of an active oligomeric state: (i) AUC data demonstrate the presence of oligomers; (ii) mutational analysis reveals a trans-arginine finger, R158, indispensable for ATP hydrolysis; (iii) the location of this arginine is conserved with the HerA/FtsK ATPase superfamily; (iv) a molecular docking model of the pentamer is compatible with the location of the identified arginine finger. However, this pentameric model is structurally incompatible with the monomeric 'initiation' state and is supported by the observed increase in kcat of ATP hydrolysis, from 7.8 ± 0.1 min-1 to 457.7 ± 9.2 min-1 upon removal of the C-terminal nuclease domain. Taken together, these structural, biophysical and biochemical data suggest a model where transition from the 'initiation' state into a catalytically competent pentameric state, is accompanied by substantial domain rearrangements, triggered by the removal of the C-terminal arm from the ATPase active site.
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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.