PLEVKA, Pavel, Susan HAFENSTEIN, Lei LI, Anthony, Jr. D'ABRAMO, Susan F. COTMORE, Michael G. ROSSMANN a Peter TATTERSALL. Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold Axis. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2011, roč. 85, č. 10, s. 4822-4827. ISSN 0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.02598-10.
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Základní údaje
Originální název Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold Axis
Autoři PLEVKA, Pavel, Susan HAFENSTEIN, Lei LI, Anthony, Jr. D'ABRAMO, Susan F. COTMORE, Michael G. ROSSMANN a Peter TATTERSALL.
Vydání JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2011, 0022-538X.
Další údaje
Originální jazyk angličtina
Typ výsledku Článek v odborném periodiku
Obor 10600 1.6 Biological sciences
Stát vydavatele Spojené státy
Utajení není předmětem státního či obchodního tajemství
Impakt faktor Impact factor: 5.402
Organizační jednotka Středoevropský technologický institut
Doi http://dx.doi.org/10.1128/JVI.02598-10
UT WoS 000289787300019
Klíčová slova anglicky VP1 N-TERMINUS; FUNCTIONAL IMPLICATIONS; CANINE PARVOVIRUS; DNA-REPLICATION; TYPE-2; PROTEIN; HELICASE; BINDING; CAPSIDS; VIRION
Štítky neMU
Změnil Změnila: Mgr. Eva Špillingová, učo 110713. Změněno: 29. 3. 2017 14:59.
Anotace
The parvovirus minute virus of mice (MVM) packages a single copy of its linear single-stranded DNA genome into preformed capsids, in a process that is probably driven by a virus-encoded helicase. Parvoviruses have a roughly cylindrically shaped pore that surrounds each of the 12 5-fold vertices. The pore, which penetrates the virion shell, is created by the juxtaposition of 10 antiparallel beta-strands, two from each of the 5-fold-related capsid proteins. There is a bottleneck in the channel formed by the symmetry-related side chains of the leucines at position 172. We report here the X-ray crystal structure of the particles produced by a leucine-to-tryptophan mutation at position 172 and the analysis of its biochemical properties. The mutant capsid had its 5-fold channel blocked, and the particles were unable to package DNA, strongly suggesting that the 5-fold pore is the packaging portal for genome entry.
VytisknoutZobrazeno: 12. 9. 2024 06:19