7PZN
wt HBc capsid like particles in complex with inhibitory peptide SLLGRM and Triton X-100
Summary for 7PZN
| Entry DOI | 10.2210/pdb7pzn/pdb |
| EMDB information | 13734 |
| Descriptor | Capsid protein, SLLGRM, modelled as poly-A,SLLGRM, modelled as poly-A, FRAGMENT OF TRITON X-100 (3 entities in total) |
| Functional Keywords | wt hbc capsid, triton x-100, inhibitory peptide sllgrm, cryo-em, hepatitis b virus, viral protein |
| Biological source | Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) More |
| Total number of polymer chains | 5 |
| Total formula weight | 87012.17 |
| Authors | Makbul, C.,Boettcher, B. (deposition date: 2021-10-12, release date: 2021-12-08, Last modification date: 2025-07-09) |
| Primary citation | Makbul, C.,Kraft, C.,Griessmann, M.,Rasmussen, T.,Katzenberger, K.,Lappe, M.,Pfarr, P.,Stoffer, C.,Stohr, M.,Wandinger, A.M.,Bottcher, B. Binding of a Pocket Factor to Hepatitis B Virus Capsids Changes the Rotamer Conformation of Phenylalanine 97. Viruses, 13:-, 2021 Cited by PubMed Abstract: (1) Background: During maturation of the Hepatitis B virus, a viral polymerase inside the capsid transcribes a pre-genomic RNA into a partly double stranded DNA-genome. This is followed by envelopment with surface proteins inserted into a membrane. Envelopment is hypothetically regulated by a structural signal that reports the maturation state of the genome. NMR data suggest that such a signal can be mimicked by the binding of the detergent Triton X 100 to hydrophobic pockets in the capsid spikes. (2) Methods: We have used electron cryo-microscopy and image processing to elucidate the structural changes that are concomitant with the binding of Triton X 100. (3) Results: Our maps show that Triton X 100 binds with its hydrophobic head group inside the pocket. The hydrophilic tail delineates the outside of the spike and is coordinated via Lys-96. The binding of Triton X 100 changes the rotamer conformation of Phe-97 in helix 4, which enables a π-stacking interaction with Trp-62 in helix 3. Similar changes occur in mutants with low secretion phenotypes (P5T and L60V) and in a mutant with a pre-mature secretion phenotype (F97L). (4) Conclusion: Binding of Triton X 100 is unlikely to mimic structural maturation because mutants with different secretion phenotypes show similar structural responses. PubMed: 34834922DOI: 10.3390/v13112115 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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