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Nucleic Acids Research Advance Access originally published online on October 24, 2006
Nucleic Acids Research 2006 34(20):5829-5838; doi:10.1093/nar/gkl708
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Nucleic Acids Research, 2006, Vol. 34, No. 20 5829-5838
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity

Alessandro Costa, Tillmann Pape1, Marin van Heel1, Peter Brick, Ardan Patwardhan1 and Silvia Onesti*

Division of Cell and Molecular Biology, Faculty of Natural Sciences,Imperial College London SW7 2AZ, UK 1 Division of Molecular Biosciences, Faculty of Natural Sciences,Imperial College London SW7 2AZ, UK

*To whom correspondence should be addressed. Tel: +44 20 7594 7647; Fax: +44 20 75890191; Email: s.onesti{at}imperial.ac.uk

Received August 4, 2006. Revised September 12, 2006. Accepted September 13, 2006.

The MCM complex from the archaeon Methanother-mobacter thermautotrophicus is a model for the eukaryotic MCM2-7 helicase. We present electron-microscopy single-particle reconstructions of a DNA treated M.thermautotrophicus MCM sample and a ADP·AlFx treated sample, respectively assembling as double hexamers and double heptamers. The electron-density maps display an unexpected asymmetry between the two rings, suggesting that large conformational changes can occur within the complex. The structure of the MCM N-terminal domain, as well as the AAA+ and the C-terminal HTH dom-ains of ZraR can be fitted into the reconstructions. Distinct configurations can be modelled for the AAA+ and the HTH domains, suggesting the nature of the conformational change within the complex. The pre-sensor 1 and the helix 2 insertions, important for the activity, can be located pointing towards the centre of the channel in the presence of DNA. We propose a mechanistic model for the helicase activity, based on a ligand-controlled rotation of the AAA+ subunits.


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