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Atomistic Ensemble Modeling and Small-Angle Neutron Scattering of Intrinsically Disordered Protein Complexes: Applied to Minichromosome Maintenance Protein

Published

Author(s)

Susan Krueger, Jae-Ho Shin, Sindhushree NMN Raghunandan, Joseph E. Curtis, Zvi Kelman

Abstract

The minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in archaea and eukarya. The solution structure of the N-terminal portion of the MCM complex from the archaeon Methanothermobacter thermautotrophicus {N-mtMCM) has been determined using small angle neutron scattering (SANS) in the presence and absence of DNA. It was found that large structural movements between the three domains of N-mtMCM occur in solution. These results provide structural support to the previously reported biochemical observations regarding the activation of the MCM helicase in archaea and eukarya.
Citation
Biophysical Journal
Volume
101

Keywords

minichromosome maintenance complex, small-angle neutron scattering, Methanothermobacter thermautotrophicus, dna binding protein, helicase

Citation

Krueger, S. , Shin, J. , , S. , Curtis, J. and Kelman, Z. (2011), Atomistic Ensemble Modeling and Small-Angle Neutron Scattering of Intrinsically Disordered Protein Complexes: Applied to Minichromosome Maintenance Protein, Biophysical Journal, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=908573 (Accessed April 18, 2024)
Created December 15, 2011, Updated February 19, 2017