Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Binding of a Pocket Factor to Hepatitis B Virus Capsids Changes the Rotamer Conformation of Phenylalanine 97.
Journal, issue, pages	Viruses, Vol. 13, Issue 11, Year 2021
Publish date	Oct 20, 2021
Authors	Cihan Makbul / Christian Kraft / Matthias Grießmann / Tim Rasmussen / Kilian Katzenberger / Melina Lappe / Paul Pfarr / Cato Stoffer / Mara Stöhr / Anna-Maria Wandinger / Bettina Böttcher /
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 ...(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.
External links	Viruses / PubMed:34834922 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.2 Å
Structure data	13726 7pz9 EMDB-13726, PDB-7pz9: HBc-F97L premature secretion phenotype Method: EM (single particle) / Resolution: 2.8 Å 13728 7pzi EMDB-13728, PDB-7pzi: HBc-F97L (premature secretion phenotype) in complex with Triton X-100 Method: EM (single particle) / Resolution: 2.9 Å 13731 7pzk EMDB-13731, PDB-7pzk: HBc-WT in complex with Triton X-100 Method: EM (single particle) / Resolution: 3.1 Å 13732 7pzl EMDB-13732, PDB-7pzl: HBc-F97L premature secretion phenotype Method: EM (single particle) / Resolution: 2.8 Å 13733 7pzm EMDB-13733, PDB-7pzm: HBc-P5T in complex with X-100 Method: EM (single particle) / Resolution: 2.9 Å 13734 7pzn EMDB-13734, PDB-7pzn: wt HBc capsid like particles in complex with inhibitory peptide SLLGRM and Triton X-100 Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-TRT: FRAGMENT OF TRITON X-100 / detergent*YM / Triton X-100
Source	Hepatitis B virus ayw/France/Tiollais/1979 hepatitis b virus genotype d subtype ayw (isolate france/tiollais/1979) escherichia coli (E. coli)
Keywords	VIRUS LIKE PARTICLE / Icosahedral capsid like particle with T=4 / VIRAL PROTEIN / Pocket binding factor mimic Triton X-100 / premature secretion phenotype / hepatitis B virus / 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 / inhibitory peptide SLLGRM / Cryo-EM