Insights into the Architecture of the Replicative Helicase from the Structure of an Archaeal MCM Homolog
| Autor: | Yuyen Lin, Silvia Onesti, Joseph S. Brunzelle, Yi Hsing Chen, Isaac K. O. Cann, Satish K. Nair, Brian Bae, Alessandro Costa |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
DNA Replication
Models Molecular Protein Conformation Archaeal Proteins Molecular Sequence Data Crystal structure 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Minichromosome maintenance Structural Biology ATP hydrolysis Catalytic Domain Hydrolase Animals Humans Amino Acid Sequence Molecular Biology 030304 developmental biology 0303 health sciences Sequence Homology Amino Acid biology DNA Helicases Nuclear Proteins Helicase Active site Minichromosome Maintenance Complex Component 2 DNA Archaea Crosstalk (biology) Eukaryotic Cells Biochemistry chemistry biology.protein Biophysics Protein Multimerization 030217 neurology & neurosurgery |
| Zdroj: | Structure. 17:211-222 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2008.11.010 |
| Popis: | SummaryThe minichromosome maintenance (MCM) proteins, members of the AAA+ (ATPase associated with diverse cellular activities) superfamily, are believed to constitute the replicative helicase in eukaryotic and archaeal species. Here, we present the 1.9 Å resolution crystal structure of a monomeric MCM homolog from Methanopyrus kandleri, the first crystallographic structure of a full-length MCM. We also present an 18 Å cryo-electron microscopy reconstruction of the hexameric MCM from Methanothermobacter thermautotrophicus, and fit the atomic resolution crystal structure into the reconstruction in order to generate an atomic model for the oligomeric assembly. These structural data reveal a distinct active site topology consisting of a unique arrangement of critical determinants. The structures also provide a molecular framework for understanding the functional contributions of trans-acting elements that facilitate intersubunit crosstalk in response to DNA binding and ATP hydrolysis. |
| Databáze: | OpenAIRE |
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