ArticleStructure (London, England : 1993)2018
A Hyperthermophilic Phage Decoration Protein Suggests Common Evolutionary Origin with Herpesvirus Triplex Proteins and an Anti-CRISPR Protein.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- TheJournal of virology · 2025Article
- Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum.Nature communications · 2025Article
- The Expanding Diversity of Viruses from Extreme Environments.International journal of molecular sciences · 2024Review
- Article
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- Structures and Strategies of Anti-CRISPR-Mediated Immune Suppression.Annual review of microbiology · 2020Review
- Phage G Structure at 6.1 Å Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus.Journal of molecular biology · 2020Article
- A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry.The Journal of biological chemistry · 2020Article
- A cornucopia of Shigella phages from the Cornhusker State.Virology · 2019Article
- Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure.Nature communications · 2019Article
- Functional metagenomics-guided discovery of potent Cas9 inhibitors in the human microbiome.eLife · 2019Article
- Keeping crispr in check: diverse mechanisms of phage-encoded anti-crisprs.FEMS microbiology letters · 2019Review
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
- Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with supersized T=7 capsids.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Potent Cas9 Inhibition in Bacterial and Human Cells by AcrIIC4 and AcrIIC5 Anti-CRISPR Proteins.mBio · 2018Article
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Authors and funding
7 authors.
Funding
Abstract
Virus capsids are protein shells that protect the viral genome from environmental assaults, while maintaining the high internal pressure of the tightly packaged genome. To elucidate how capsids maintain stability under harsh conditions, we investigated the capsid components of the hyperthermophilic phage P74-26. We determined the structure of capsid protein gp87 and show that it has the same fold as decoration proteins in many other phages, despite lacking significant sequence homology. We also find that gp87 is significantly more stable than mesophilic homologs. Our analysis of the gp87 structure reveals that the core "β tulip" domain is conserved in trimeric capsid components across numerous double-stranded DNA viruses, including Herpesviruses. Moreover, this β barrel domain is found in anti-CRISPR protein AcrIIC1, suggesting a mechanism for the evolution of this Cas9 inhibitor. Our work illustrates the principles for increased stability of gp87, and extends the evolutionary reach of the β tulip domain.
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