ArticleJournal of molecular biology2014
Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid.Nature communications · 2025Article
- Encapsulin cargo loading: progress and potential.Journal of materials chemistry. B · 2023Review
- A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.Structure (London, England : 1993) · 2023Article
- Triggered Reversible Disassembly of an Engineered Protein Nanocage*.Angewandte Chemie (International ed. in English) · 2021Article
- Advances in encapsulin nanocompartment biology and engineering.Biotechnology and bioengineering · 2021Review
- Capsids and Portals Influence Each Other's Conformation During Assembly and Maturation.Journal of molecular biology · 2020Article
- Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- A Hydrophobic Network: Intersubunit and Intercapsomer Interactions Stabilizing the Bacteriophage P22 Capsid.Journal of virology · 2019Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.Journal of molecular biology · 2017Article
- Article
- Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.Nature structural & molecular biology · 2016Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Protein chainmail variants in dsDNA viruses.AIMS biophysics · 2015Article
- Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.Structure (London, England : 1993) · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The G-loop is a 10-residue glycine-rich loop that protrudes from the surface of the mature bacteriophage HK97 capsid at the C-terminal end of the long backbone helix of major capsid protein subunits. The G-loop is essential for assembly, is conserved in related capsid and encapsulin proteins, and plays its role during HK97 capsid assembly by making crucial contacts between the hill-like hexamers and pentamers in precursor proheads. These contacts are not preserved in the flattened capsomers of the mature capsid. Aspartate 231 in each of the ~400 G-loops interacts with lysine 178 of the E-loop (extended loop) of a subunit on an adjacent capsomer. Mutations disrupting this interaction prevented correct assembly and, in some cases, induced abnormal assembly into tubes, or small, incomplete capsids. Assembly remained defective when D231 and K178 were replaced with larger charged residues or when their positions were exchanged. Second-site suppressors of lethal mutants containing substitution D231L replaced the ionic interaction with new interactions between neutral and hydrophobic residues of about the same size: D231L/K178V, D231L/K178I, and D231L/K178N. We conclude that it is not the charge but the size and shape of the side chains of residues 178 and 231 that are important. These two residues control the geometry of contacts between the E-loop and the G-loop, which apparently must be precisely spaced and oriented for correct assembly to occur. We present a model for how the G-loop could control HK97 assembly and identify G-loop-like protrusions in other capsid proteins that may play analogous roles.
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