Discover Community Create You

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

Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage Chi.

Biochemistry - 27 Feb 1996

Hwang Y, Catalano C E, Feiss M

Abstract excerpt

Terminase the DNA packaging enzyme of bacteriophage chi, is a heteromultimer of gpNul (21 kDa) and gpA (74 kDa) subunits, encoded by the chi Nul and A genes, respectively. Sequence comparisons indicate that both gpNu1 and gpA have a match to the P-loop motif of ATPase centers, which is a glycine-rich segment followed by a lysine. By site-specific mutagenesis, we changed the lysines of the putative P-loops of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Genes, Viral
Share to Kinetics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Molecular Weight

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 8611586
DOI: 10.1021/bi952322z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage Chi.PMID 8611586Read ↗

ATPase center of bacteriophage lambda terminase involved in post-cleavage stages of DNA packaging: identification of ATP-interactive amino acids.Semantic proximity Read ↗

Mutations affecting the high affinity ATPase center of gpA, the large subunit of bacteriophage lambda terminase, inactivate the endonuclease activity of terminase.Semantic proximity Read ↗

The DNA maturation domain of gpA, the DNA packaging motor protein of bacteriophage lambda, contains an ATPase site associated with endonuclease activity.Semantic proximity Read ↗

The large subunit of bacteriophage lambda's terminase plays a role in DNA translocation and packaging termination.Semantic proximity Read ↗

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

Novel and deviant Walker A ATP-binding motifs in bacteriophage large terminase-DNA packaging proteins.Semantic proximity Read ↗

Analysis of a mutation affecting the specificity domain for prohead binding of the bacteriophage lambda terminase.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 ↗

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 ↗

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

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 ↗

Mutations in the terminase genes of bacteriophage lambda that bypass the necessity for FI.Semantic proximity Read ↗

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