Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex.
Nucleic Acids Res
; 43(5): 2958-67, 2015 Mar 11.
Article
em En
| MEDLINE
| ID: mdl-25712103
ABSTRACT
The minichromosome maintenance complex (MCM) represents the replicative DNA helicase both in eukaryotes and archaea. Here, we describe the solution structure of the C-terminal domains of the archaeal MCMs of Sulfolobus solfataricus (Sso) and Methanothermobacter thermautotrophicus (Mth). Those domains consist of a structurally conserved truncated winged helix (WH) domain lacking the two typical 'wings' of canonical WH domains. A less conserved N-terminal extension links this WH module to the MCM AAA+ domain forming the ATPase center. In the Sso MCM this linker contains a short α-helical element. Using Sso MCM mutants, including chimeric constructs containing Mth C-terminal domain elements, we show that the ATPase and helicase activity of the Sso MCM is significantly modulated by the short α-helical linker element and by N-terminal residues of the first α-helix of the truncated WH module. Finally, based on our structural and functional data, we present a docking-derived model of the Sso MCM, which implies an allosteric control of the ATPase center by the C-terminal domain.
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Base de dados:
MEDLINE
Assunto principal:
Estrutura Terciária de Proteína
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Estrutura Secundária de Proteína
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Proteínas Arqueais
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Proteínas de Manutenção de Minicromossomo
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article