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Nucleic Acids Research Advance Access published online on April 16, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn183
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© 2008 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 analysis of the Sulfolobus solfataricus MCM protein N-terminal domain{dagger}

Wei Liu1,*, Biagio Pucci2, Mosè Rossi2, Francesca M. Pisani2 and Rudolf Ladenstein1

1Center of Structural Biochemistry, Karolinska Institutet NOVUM, 141 57 Huddinge, Sweden and 2Institute of Protein Biochemistry–CNR, Via P. Castellino, 111. 80131-Naples, Italy

*To whom correspondence should be addressed. Tel: +46 8 6089178; Fax: +46 8 6089290; Email: wei.liu{at}ki.se Correspondence may also be addressed to Francesca M. Pisani. Tel: +39 816132292; Fax: +39 816132277; Email: fm.pisani{at}ibp.cnr.it {dagger}Data deposition: The coordinates of the structure in space group C2 have been deposited into Protein Data Bank with a PDBID 2VL6 Present address: Biagio Pucci, Centro Ricerche Oncologiche Mercogliano (Fondazione Pascale). Mercogliano (AV), Italy

Received March 6, 2008. Revised March 27, 2008. Accepted March 28, 2008.

The Mini-Chromosome Maintenance (MCM) proteins are candidates of replicative DNA helicase in eukarya and archaea. Here we report a 2.8 Å crystal structure of the N-terminal domain (residues 1–268) of the Sulfolobus solfataricus MCM (Sso MCM) protein. The structure reveals single-hexameric ring-like architecture, at variance from the protein of Methanothermobacter thermoautotrophicus (Mth). Moreover, the central channel in Sso MCM seems significantly narrower than the Mth counterpart, which appears to more favorably accommodate single-stranded DNA than double-stranded DNA, as supported by DNA-binding assays. Structural analysis also highlights the essential role played by the zinc-binding domain in the interaction with nucleic acids and allows us to speculate that the Sso MCM N-ter domain may function as a molecular clamp to grasp the single-stranded DNA passing through the central channel. On this basis possible DNA unwinding mechanisms are discussed.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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