Summary for 6CGV
| Entry DOI | 10.2210/pdb6cgv/pdb |
| Related | 6b1t |
| Descriptor | Hexon protein, Penton protein, Pre-hexon-linking protein IIIa, ... (6 entities in total) |
| Functional Keywords | human adenovirus crystal structure ad5f35 ad35f, virus |
| Biological source | Human adenovirus C serotype 5 (HAdV-5) More |
| Total number of polymer chains | 21 |
| Total formula weight | 1532273.95 |
| Authors | Natchiar, S.K.,Venkataraman, S.,Nemerow, G.R.,Reddy, V.S. (deposition date: 2018-02-21, release date: 2018-04-25, Last modification date: 2024-10-30) |
| Primary citation | Kundhavai Natchiar, S.,Venkataraman, S.,Mullen, T.M.,Nemerow, G.R.,Reddy, V.S. Revised Crystal Structure of Human Adenovirus Reveals the Limits on Protein IX Quasi-Equivalence and on Analyzing Large Macromolecular Complexes. J. Mol. Biol., 430:4132-4141, 2018 Cited by PubMed Abstract: We report the revised crystal structure of a pseudo-typed human adenovirus at 3.8-Å resolution that is consistent with the atomic models of minor proteins determined by cryo-electron microscopy. The diffraction data from multiple crystals were rescaled and merged to increase the data completeness. The densities for the minor proteins were initially identified in the phase-refined omit maps that were further improved by the phases from docked poly-alanine models to build atomic structures. While the trimeric fiber molecules are disordered due to flexibility and imposition of 5-fold symmetry, the remaining major capsid proteins hexon and penton base are clearly ordered, with the exception of hypervariable region 1 of hexons, the RGD containing loop, and the N-termini of the penton base. The exterior minor protein IX together with the interior minor proteins IIIa and VIII stabilizes the adenovirus virion. A segment of N-terminal pro-peptide of VI is found in the interior cavities of peripentonal hexons, and the rest of VI is disordered. While the triskelion substructures formed by the N-termini of IX conform to excellent quasi 3-fold symmetry, the tetrameric coiled-coils formed by the C-termini and organized in parallel and anti-parallel arrangement do not exhibit any quasi-symmetry. This observation also conveys the pitfalls of using the quasi-equivalence as validation criteria for the structural analysis of extended (non-modular) capsid proteins such as IX. Together, these results remedy certain discrepancies in the previous X-ray model in agreement with the cryo-electron microscopy models. PubMed: 30121295DOI: 10.1016/j.jmb.2018.08.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.8 Å) |
Structure validation
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