9E99
Cryo-EM reconstruction of Escherichia phage N4 capsid
Summary for 9E99
| Entry DOI | 10.2210/pdb9e99/pdb |
| EMDB information | 47777 |
| Descriptor | Major capsid protein, 32 kDa protein (2 entities in total) |
| Functional Keywords | bacteriophage, capsid, hoc-like decoration protein, ig-like decoration protein, schitoviridae, n4, enquatroviridae, viral protein |
| Biological source | Escherichia phage N4 More |
| Total number of polymer chains | 12 |
| Total formula weight | 484291.04 |
| Authors | Eruera, A.,McJarrow-Keller, K.,Hyun, J.K.,Bostina, M. (deposition date: 2024-11-07, release date: 2025-02-19) |
| Primary citation | McJarrow-Keller, K.,Eruera, A.R.,Crowe, A.J.M.,Kumaran, R.,Hyun, J.,Bostina, M. Atlas of Interactions Between Decoration Proteins and Major Capsid Proteins of Coliphage N4. Viruses, 17:-, 2024 Cited by PubMed Abstract: Coliphage N4 is a representative species of the family of bacteriophages. Originally structurally studied in 2008, the capsid structure was solved to 14 Å to reveal an interesting arrangement of Ig-like decoration proteins across the surface of the capsid. Herein, we present a high-resolution N4 structure, reporting a 2.45 Å map of the capsid obtained via single particle cryogenic-electron microscopy. Structural analysis of the major capsid proteins (MCPs) and decoration proteins (gp56 and gp17) of phage N4 reveals a pattern of interactions across the capsid that are mediated by structurally homologous domains of gp17. In this study, an analysis of the complex interface contacts allows us to confirm that the gp17 Ig-like decoration proteins of N4 are likely employed by the virus to increase the capsid's structural integrity. PubMed: 39861808DOI: 10.3390/v17010019 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.45 Å) |
Structure validation
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