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@article{842971,
author = {Macek, Pavel and Chmelík, Josef and Křížová, Ivana and Kadeřávek, Pavel and Padrta, Petr and Žídek, Lukáš and Wildová, Marcela and Hadravová, Romana and Chaloupková, Radka and Pichová, Iva and Ruml, Tomáš and Rumlová, Michaela and Sklenář, Vladimír},
article_number = {1},
keywords = {M-PMV; betaretroviruses; capsid protein; NMR structure; internal dynamics},
language = {eng},
issn = {0022-2836},
journal = {Journal of Molecular Biology},
title = {NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus},
volume = {392},
year = {2009}
}
TY - JOUR
ID - 842971
AU - Macek, Pavel - Chmelík, Josef - Křížová, Ivana - Kadeřávek, Pavel - Padrta, Petr - Žídek, Lukáš - Wildová, Marcela - Hadravová, Romana - Chaloupková, Radka - Pichová, Iva - Ruml, Tomáš - Rumlová, Michaela - Sklenář, Vladimír
PY - 2009
TI - NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus
JF - Journal of Molecular Biology
VL - 392
IS - 1
SP - 100
EP - 100
SN - 00222836
KW - M-PMV
KW - betaretroviruses
KW - capsid protein
KW - NMR structure
KW - internal dynamics
N2 - The high-resolution structure of the N-terminal domain (NTD) of the retroviral capsid protein (CA) of Mason-Pfizer monkey virus (M-PMV), a member of the betaretrovirus family, has been determined by NMR. The M-PMV NTD CA structure is similar to the other retroviral capsid structures and is characterized by a six alpha-helix bundle and an N-terminal beta-hairpin, stabilized by an interaction of highly conserved residues, Pro1 and Asp57. Since the role of the beta-hairpin has been shown to be critical for formation of infectious viral core, we also investigated the functional role of M-PMV beta-hairpin in two mutants (i.e., DeltaP1NTDCA and D57ANTDCA) where the salt bridge stabilizing the wild-type structure was disrupted. NMR data obtained for these mutants were compared with those obtained for the wild type. The main structural changes were observed within the beta-hairpin structure; within helices 2, 3, and 5; and in the loop connecting helices 2 and 3. This observation is supported by biochemical data showing different cleavage patterns of the wild-type and the mutated capsid-nucleocapsid fusion protein (CANC) by M-PMV protease. Despite these structural changes, the mutants with disrupted salt bridge are still able to assemble into immature, spherical particles. This confirms that the mutual interaction and topology within the beta-hairpin and helix 3 might correlate with the changes in interaction between immature and mature lattices.
ER -
MACEK, Pavel, Josef CHMELÍK, Ivana KŘÍŽOVÁ, Pavel KADEŘÁVEK, Petr PADRTA, Lukáš ŽÍDEK, Marcela WILDOVÁ, Romana HADRAVOVÁ, Radka CHALOUPKOVÁ, Iva PICHOVÁ, Tomáš RUML, Michaela RUMLOVÁ a Vladimír SKLENÁŘ. NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus. \textit{Journal of Molecular Biology}. 2009, roč.~392, č.~1, s.~100-114. ISSN~0022-2836.
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