7PZM

HBc-P5T in complex with X-100

7PZM の概要

• エントリーDOI: 10.2210/pdb7pzm/pdb
• EMDBエントリー: 13733
• 分子名称: Capsid protein, FRAGMENT OF TRITON X-100 (2 entities in total)
• 機能のキーワード: hbc-p5t (low secretion phenotype) in complex with triton x-100, viral protein
• 由来する生物種: Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 86010.85

構造登録者

Makbul, C.,Boettcher, B. (登録日: 2021-10-12, 公開日: 2021-12-08, 最終更新日: 2025-07-09)

主引用文献

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

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: 34834922
DOI: 10.3390/v13112115

実験手法

ELECTRON MICROSCOPY (2.9 Å)