Skip Navigation


Nucleic Acids Research Advance Access originally published online on April 16, 2008
Nucleic Acids Research 2008 36(10):3235-3243; doi:10.1093/nar/gkn183
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (4880K) Freely available
Right arrow Screen PDF (641K) Freely available
Right arrowOA All Versions of this Article:
36/10/3235    most recent
gkn183v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (1)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Liu, W.
Right arrow Articles by Ladenstein, R.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Liu, W.
Right arrow Articles by Ladenstein, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2008, Vol. 36, No. 10 3235-3243
© 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

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.

{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

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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.