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

Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage phiYY.

International journal of biological macromolecules - 1 Jan 2022

Zhang Caiying, Li Yuelong, Samad Abdus, Zheng Peiyi, Ji Zheng, Chen Feng, Zhang Huidong, Jin Tengchuan

Abstract excerpt

phiYY is a foremost member of Cystoviridae isolated from Pseudomonas aeruginosa. Its P4 protein with NTPase activity is a molecular motor for their genome packing during viral particle assembly. Previously studies on the P4 from four Pseudomonas phages phi6, phi8, phi12 and phi13 reveal that despite of belonging to the same protein family, they are unique in sequence, structure and biochemical properties. To...

Read the complete abstract on PubMed

Topics

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

Share to Cloning, Molecular
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Protein Conformation

Share to Protein Multimerization

Share to Pseudomonas aeruginosa

Share to Structure-Activity Relationship

Share to Viral Proteins

Source

Identifiers

PMID: 34856215
DOI: 10.1016/j.ijbiomac.2021.11.129

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage phiYY.PMID 34856215Read ↗

Cryo-EM analysis of Pseudomonas phage Pa193 structural componentsSemantic proximity Read ↗

Structural basis for repurposing a flexible phage tail into an Intraspecific bacterial competition weaponSemantic proximity Read ↗

High-resolution cryo-EM analysis of the therapeutic <i>Pseudomonas</i> phage Pa223Semantic proximity Read ↗

A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filamentsSemantic proximity Read ↗

Comparative analysis of the widespread and conserved PB1-like viruses infecting Pseudomonas aeruginosa.Semantic proximity Read ↗

Structural and functional analysis of pyocin S8 from <i>Pseudomonas aeruginosa</i> : requirement of a glutamate in the H-N-H motif for the DNase activitySemantic proximity Read ↗

Structures of three actinobacteriophage capsids: Roles of symmetry and accessory proteinsSemantic proximity Read ↗

Tapping the nucleotide pool of the host: novel nucleotide carrier proteins of <i>Protochlamydia amoebophila</i>Semantic proximity Read ↗

Insights into Genome Ejection by a Therapeutic phiKMV-like BacteriophageSemantic proximity Read ↗

Inner-membrane GspF of the bacterial type II secretion system is a dimeric adaptor mediating pseudopilus biogenesisSemantic proximity Read ↗

Structures of the Ultra-High-Affinity Protein-Protein Complexes of Pyocins S2 and AP41 and Their Cognate Immunity Proteins from Pseudomonas aeruginosa.Semantic proximity Read ↗

Structural analysis of the active site architecture of the VapC toxin from Shigella flexneri.Semantic proximity Read ↗

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