5G5N
Structure of the snake adenovirus 1 hexon-interlacing LH3 protein, methylmercury chloride derivative
Summary for 5G5N
| Entry DOI | 10.2210/pdb5g5n/pdb |
| Related | 5G5O |
| Descriptor | LH3 HEXON-INTERLACING CAPSID PROTEIN, GLYCEROL, METHYL MERCURY ION, ... (5 entities in total) |
| Functional Keywords | viral protein, capsid protein, beta-helix |
| Biological source | SNAKE ADENOVIRUS 1 |
| Cellular location | Virion : A9CB85 |
| Total number of polymer chains | 3 |
| Total formula weight | 117064.15 |
| Authors | Nguyen, T.H.,Singh, A.K.,Albala-Perez, B.,van Raaij, M.J. (deposition date: 2016-05-26, release date: 2017-06-07, Last modification date: 2024-05-08) |
| Primary citation | Menendez-Conejero, R.,Nguyen, T.H.,Singh, A.K.,Condezo, G.N.,Marschang, R.E.,van Raaij, M.J.,San Martin, C. Structure of a Reptilian Adenovirus Reveals a Phage Tailspike Fold Stabilizing a Vertebrate Virus Capsid. Structure, 25:1562-1573, 2017 Cited by PubMed Abstract: Although non-human adenoviruses (AdVs) might offer solutions to problems posed by human AdVs as therapeutic vectors, little is known about their basic biology. In particular, there are no structural studies on the complete virion of any AdV with a non-mammalian host. We combine mass spectrometry, cryo-electron microscopy, and protein crystallography to characterize the composition and structure of a snake AdV (SnAdV-1, Atadenovirus genus). SnAdV-1 particles contain the genus-specific proteins LH3, p32k, and LH2, a previously unrecognized structural component. Remarkably, the cementing protein LH3 has a trimeric β helix fold typical of bacteriophage host attachment proteins. The organization of minor coat proteins differs from that in human AdVs, correlating with higher thermostability in SnAdV-1. These findings add a new piece to the intriguing puzzle of virus evolution, hint at the use of cell entry pathways different from those in human AdVs, and will help development of new, thermostable SnAdV-1-based vectors. PubMed: 28943338DOI: 10.1016/j.str.2017.08.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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