2M45

NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus

Summary for 2M45

• Entry DOI: 10.2210/pdb2m45/pdb
• NMR Information: BMRB: 18986
• Descriptor: Minichromosome maintenance protein MCM (1 entity in total)
• Functional Keywords: minichromosome maintenance protein, mcm, winged helix, hydrolase, helix-turn-helix, winged helix turn, dna helicase, thermophile proteins, pre-replicative complex, replication
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 1
• Total formula weight: 9674.41

Authors

Wiedemann, C.,Ohlenschlager, O.,Medagli, B.,Onesti, S.,Gorlach, M. (deposition date: 2013-01-29, release date: 2014-01-29, Last modification date: 2024-10-30)

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

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: 25712103
DOI: 10.1093/nar/gkv120

Experimental method

SOLUTION NMR