ArticleStructure (London, England : 1993)2014
Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed.
- Eradication of catheter-associated MDR Acinetobacter baumannii biofilms mediated by novel phage encoded depolymerase activity.NPJ biofilms and microbiomes · 2026Article
- The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMRMolecules (Basel, Switzerland) · 2024Article
- Assembly and Capsid Expansion Mechanism of Bacteriophage P22 Revealed by High-Resolution Cryo-EM Structures.Viruses · 2023Article
- Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22.Viruses · 2022Article
- Pulse-field gradient nuclear magnetic resonance of protein translational diffusion from native to non-native states.Protein science : a publication of the Protein Society · 2022Article
- Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use.Journal of biomedical science · 2022Article
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- Portal Protein: The Orchestrator of Capsid Assembly for the dsDNA Tailed Bacteriophages and Herpesviruses.Annual review of virology · 2019Review
- Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages.Journal of virology · 2019Article
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
- Comparing Hydrogen Deuterium Exchange and Fast Photochemical Oxidation of Proteins: a Structural Characterisation of Wild-Type and ΔN6 βJournal of the American Society for Mass Spectrometry · 2018Article
- The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence.Scientific reports · 2017Article
- Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.Journal of molecular biology · 2017Article
- A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.Science advances · 2017Article
- Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150.Science (New York, N.Y.) · 2017Article
- Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- NMR assignments for the insertion domain of bacteriophage Sf6 coat protein.Biomolecular NMR assignments · 2017Article
- Accurate model annotation of a near-atomic resolution cryo-EM map.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique insertion domain (I-domain). Two prior I-domain models from subnanometer cryoelectron microscopy (cryoEM) reconstructions differed substantially. Therefore, the I-domain's nuclear magnetic resonance structure was determined and also used to improve cryoEM models of coat protein. The I-domain has an antiparallel six-stranded β-barrel fold, not previously observed in HK97-fold accessory domains. The D-loop, which is dynamic in the isolated I-domain and intact monomeric coat protein, forms stabilizing salt bridges between adjacent capsomers in procapsids. The S-loop is important for capsid size determination, likely through intrasubunit interactions. Ten of 18 coat protein temperature-sensitive-folding substitutions are in the I-domain, indicating its importance in folding and stability. Several are found on a positively charged face of the β-barrel that anchors the I-domain to a negatively charged surface of the coat protein HK97-core.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.