EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Binding of a Pocket Factor to Hepatitis B Virus Capsids Changes the Rotamer Conformation of Phenylalanine 97.
ジャーナル・号・ページ	Viruses, Vol. 13, Issue 11, Year 2021
掲載日	2021年10月20日
著者	Cihan Makbul / Christian Kraft / Matthias Grießmann / Tim Rasmussen / Kilian Katzenberger / Melina Lappe / Paul Pfarr / Cato Stoffer / Mara Stöhr / Anna-Maria Wandinger / Bettina Böttcher /
PubMed 要旨	(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 ...(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.
リンク	Viruses / PubMed:34834922 / PubMed Central
手法	EM (単粒子)
解像度	2.8 - 3.2 Å
構造データ	13726 7pz9 EMDB-13726, PDB-7pz9: HBc-F97L premature secretion phenotype 手法: EM (単粒子) / 解像度: 2.8 Å 13728 7pzi EMDB-13728, PDB-7pzi: HBc-F97L (premature secretion phenotype) in complex with Triton X-100 手法: EM (単粒子) / 解像度: 2.9 Å 13731 7pzk EMDB-13731, PDB-7pzk: HBc-WT in complex with Triton X-100 手法: EM (単粒子) / 解像度: 3.1 Å 13732 7pzl EMDB-13732, PDB-7pzl: HBc-F97L premature secretion phenotype 手法: EM (単粒子) / 解像度: 2.8 Å 13733 7pzm EMDB-13733, PDB-7pzm: HBc-P5T in complex with X-100 手法: EM (単粒子) / 解像度: 2.9 Å 13734 7pzn EMDB-13734, PDB-7pzn: wt HBc capsid like particles in complex with inhibitory peptide SLLGRM and Triton X-100 手法: EM (単粒子) / 解像度: 3.2 Å
化合物	ChemComp-TRT: FRAGMENT OF TRITON X-100 / 可溶化剤*YM / トリトンX-100
由来	Hepatitis B virus ayw/France/Tiollais/1979 (B型肝炎ウイルス) hepatitis b virus genotype d subtype ayw (isolate france/tiollais/1979) (B型肝炎ウイルス) escherichia coli (大腸菌)
キーワード	VIRUS LIKE PARTICLE (ウイルス様粒子) / Icosahedral capsid like particle with T=4 / VIRAL PROTEIN (ウイルスタンパク質) / Pocket binding factor mimic Triton X-100 / premature secretion phenotype / hepatitis B virus (B型肝炎ウイルス) / HBc-WT in complex with Triton X-100 / HBc-L60V (low secretion phenotype) in complex with Triton X-100 / HBc-P5T (low secretion phenotype) in complex with Triton X-100 / wt HBc capsid / Triton X-100 (トリトンX-100) / inhibitory peptide SLLGRM / Cryo-EM (低温電子顕微鏡法)