2MA3
NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus
Summary for 2MA3
| Entry DOI | 10.2210/pdb2ma3/pdb |
| NMR Information | BMRB: 19187 |
| Descriptor | DNA replication initiator (Cdc21/Cdc54) (1 entity in total) |
| Functional Keywords | minichromosome maintenance protein, mcm, winged helix, replication |
| Biological source | Methanothermobacter thermautotrophicus (Methanothermobacter thermautotrophicus) |
| Total number of polymer chains | 1 |
| Total formula weight | 10135.65 |
| Authors | Wiedemann, C.,Ohlenschlager, O.,Medagli, B.,Onesti, S.,Gorlach, M. (deposition date: 2013-06-26, release date: 2014-12-31, Last modification date: 2024-05-15) |
| Primary citation | Wiedemann, C.,Szambowska, A.,Hafner, S.,Ohlenschlager, O.,Guhrs, K.H.,Gorlach, M. Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex. Nucleic Acids Res., 43:2958-2967, 2015 Cited by PubMed 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. PubMed: 25712103DOI: 10.1093/nar/gkv120 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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