Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional analysis of the DNA-packaging/terminase protein gp17 from bacteriophage T4.

Journal of molecular biology - 4 Sept 1998

Kuebler D, Rao V B

Abstract excerpt

In bacteriophage T4, the terminase complex constituted by the large subunit gp17 (69 kDa) and the small subunit gp16 (18 kDa) is a critical component of the ATP-driven DNA-packaging pump that translocates DNA into an empty capsid shell. Evidence suggests that the large subunit gp17 is the critica...

Topics

Adenosine Triphosphate
Bacteriophage T4
Binding Sites
Cloning, Molecular
DNA, Viral
Endodeoxyribonucleases
Histidine
Metals
Microscopy, Electron
Mutagenesis
Mutation
Viral Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 9719636
DOI: 10.1006/jmbi.1998.1952

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9719636-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of the DNA-packaging/terminase protein gp17 from bacteriophage T4.PMID 9719636Read ↗

Defining the bacteriophage T4 DNA packaging machine: evidence for a C-terminal DNA cleavage domain in the large terminase/packaging protein gp17.Semantic proximity Read ↗

The N-terminal ATPase site in the large terminase protein gp17 is critically required for DNA packaging in bacteriophage T4.Semantic proximity Read ↗

Functional analysis of the bacteriophage T4 DNA-packaging ATPase motor.Semantic proximity Read ↗

Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases.Semantic proximity Read ↗

Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.Semantic proximity Read ↗

A critical coiled coil motif in the small terminase, gp16, from bacteriophage T4: insights into DNA packaging initiation and assembly of packaging motor.Semantic proximity Read ↗

The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.Semantic proximity Read ↗

Bacteriophage T4 gene 17 amplification mutants: evidence for initiation by the T4 terminase subunit gp16.Semantic proximity Read ↗

Designing a nine cysteine-less DNA packaging motor from bacteriophage T4 reveals new insights into ATPase structure and function.Semantic proximity Read ↗

Specific interaction of terminase, the DNA packaging enzyme of bacteriophage lambda, with the portal protein of the prohead.Semantic proximity Read ↗

The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-binding protein modulates DNA binding and interaction with T7 DNA polymerase.Semantic proximity Read ↗

Isolation and characterization of the herpes simplex virus 1 terminase complex.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.