MACEK, Pavel, Josef CHMELÍK, Ivana KŘÍŽOVÁ, Pavel KADEŘÁVEK, Petr PADRTA, Lukáš ŽÍDEK, Marcela WILDOVÁ, Romana HADRAVOVÁ, Radka CHALOUPKOVÁ, Iva PICHOVÁ, Tomáš RUML, Michaela RUMLOVÁ and Vladimír SKLENÁŘ. NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus. Journal of Molecular Biology. 2009, vol. 392, No 1, p. 100-114. ISSN 0022-2836.
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Basic information
Original name NMR Structure of the N-Terminal Domain of Capsid Protein from the Mason-Pfizer Monkey Virus
Name in Czech NMR struktura N-terminální domény kapsidového proteinu Mason-Pfizerova opičího viru
Authors MACEK, Pavel (203 Czech Republic, belonging to the institution), Josef CHMELÍK (203 Czech Republic, belonging to the institution), Ivana KŘÍŽOVÁ (203 Czech Republic), Pavel KADEŘÁVEK (203 Czech Republic), Petr PADRTA (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution), Marcela WILDOVÁ (203 Czech Republic), Romana HADRAVOVÁ (203 Czech Republic), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Iva PICHOVÁ (203 Czech Republic), Tomáš RUML (203 Czech Republic), Michaela RUMLOVÁ (203 Czech Republic) and Vladimír SKLENÁŘ (203 Czech Republic, guarantor, belonging to the institution).
Edition Journal of Molecular Biology, 2009, 0022-2836.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.871
RIV identification code RIV/00216224:14310/09:00036514
Organization unit Faculty of Science
UT WoS 000270123600008
Keywords in English M-PMV; betaretroviruses; capsid protein; NMR structure; internal dynamics
Tags International impact, Reviewed
Changed by Changed by: prof. RNDr. Vladimír Sklenář, DrSc., učo 2611. Changed: 10/3/2011 13:05.
Abstract
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.
Abstract (in Czech)
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.
Links
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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