4V4U
The quasi-atomic model of Human Adenovirus type 5 capsid
This is a non-PDB format compatible entry.
Summary for 4V4U
| Entry DOI | 10.2210/pdb4v4u/pdb |
| Related | 1X9P 1X9T |
| EMDB information | 1111 1112 1113 |
| Descriptor | PENTON PROTEIN, N-TERMINAL PEPTIDE OF FIBER PROTEIN, HEXON PROTEIN (3 entities in total) |
| Functional Keywords | virus, adenovirus, minor capsid protein, quasi atomic |
| Biological source | HUMAN ADENOVIRUS 2 More |
| Total number of polymer chains | 22 |
| Total formula weight | 1592891.96 |
| Authors | Fabry, C.M.S.,Rosa-Calatrava, M.,Conway, J.F.,Zubieta, C.,Cusack, S.,Ruigrok, R.W.H.,Schoehn, G. (deposition date: 2005-03-03, release date: 2014-07-09, Last modification date: 2024-05-08) |
| Primary citation | Fabry, C.M.S.,Rosa-Calatrava, M.,Conway, J.F.,Zubieta, C.,Cusack, S.,Ruigrok, R.W.H.,Schoehn, G. A Quasi-Atomic Model of Human Adenovirus Type 5 Capsid. Embo J., 24:1645-, 2005 Cited by PubMed Abstract: Adenoviruses infect a wide range of vertebrates including humans. Their icosahedral capsids are composed of three major proteins: the trimeric hexon forms the facets and the penton, a noncovalent complex of the pentameric penton base and trimeric fibre proteins, is located at the 12 capsid vertices. Several proteins (IIIa, VI, VIII and IX) stabilise the capsid. We have obtained a 10 A resolution map of the human adenovirus 5 by image analysis from cryo-electron micrographs (cryoEMs). This map, in combination with the X-ray structures of the penton base and hexon, was used to build a quasi-atomic model of the arrangement of the two major capsid components and to analyse the hexon-hexon and hexon-penton interactions. The secondary proteins, notably VIII, were located by comparing cryoEM maps of native and pIX deletion mutant virions. Minor proteins IX and IIIa are located on the outside of the capsid, whereas protein VIII is organised with a T=2 lattice on the inner face of the capsid. The capsid organisation is compared with the known X-ray structure of bacteriophage PRD1. PubMed: 15861131DOI: 10.1038/SJ.EMBOJ.7600653 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (10 Å) |
Structure validation
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