ArticleMolecular & cellular proteomics : MCP2010
A docking model based on mass spectrometric and biochemical data describes phage packaging motor incorporation.
Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- A highly conserved basic motif in the wing domain of portal protein is necessary for oligomerization and incorporation in phage P22.Journal of virology · 2026Article
- Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation.Journal of molecular biology · 2024Article
- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Structure and host specificity ofScience advances · 2022Article
- Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22.Viruses · 2022Article
- Cryo-EM Structure of a Kinetically Trapped Dodecameric Portal Protein from the Pseudomonas-phage PaP3.Journal of molecular biology · 2022Article
- Article
- Portal Protein: The Orchestrator of Capsid Assembly for the dsDNA Tailed Bacteriophages and Herpesviruses.Annual review of virology · 2019Review
- A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.Science advances · 2017Article
- Cryo-EM Data Are Superior to Contact and Interface Information in Integrative Modeling.Biophysical journal · 2016Article
- Proteomic approaches to uncovering virus-host protein interactions during the progression of viral infection.Expert review of proteomics · 2016Review
- Diverse self-association properties within a family of phage packaging RNAs.RNA (New York, N.Y.) · 2014Article
- A mass spectrometry view of stable and transient protein interactions.Advances in experimental medicine and biology · 2014Review
- Quantitative cross-linking/mass spectrometry using isotope-labelled cross-linkers.Journal of proteomics · 2013Article
- Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.Analytical chemistry · 2013Review
- Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions.Journal of proteome research · 2012Article
- The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination.Journal of molecular biology · 2011Article
- Modern biomolecular mass spectrometry and its role in studying virus structure, dynamics, and assembly.Angewandte Chemie (International ed. in English) · 2011Review
- The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes.Journal of structural biology · 2011Article
- Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The molecular mechanism of scaffolding protein-mediated incorporation of one and only one DNA packaging motor/connector dodecamer at a unique vertex during lambdoid phage assembly has remained elusive because of the lack of structural information on how the connector and scaffolding proteins interact. We assembled and characterized a phi29 connector-scaffolding complex, which can be incorporated into procapsids during in vitro assembly. Native mass spectrometry revealed that the connector binds at most 12 scaffolding molecules, likely organized as six dimers. A data-driven docking model, using input from chemical cross-linking and mutagenesis data, suggested an interaction between the scaffolding protein and the exterior of the wide domain of the connector dodecamer. The connector binding region of the scaffolding protein lies upstream of the capsid binding region located at the C terminus. This arrangement allows the C terminus of scaffolding protein within the complex to both recruit capsid subunits and mediate the incorporation of the single connector vertex.
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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.