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Nucleic Acids Research 2006 34(5):1439-1449; doi:10.1093/nar/gkl009
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Published online 9 March 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Structural insight into gene transcriptional regulation and effector binding by the Lrp/AsnC family

Paul Thaw, Svetlana E. Sedelnikova, Tatyana Muranova, Sebastian Wiese, Sylvia Ayora1,2, Juan C. Alonso2, Arie B. Brinkman3, Jasper Akerboom4, John van der Oost4 and John B. Rafferty*

Department of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield Western Bank, Sheffield S10 2TN, UK 1Departamento de Biologia Molecular, Universidad Autonoma de Madrid Cantoblanco, 28049 Madrid, Spain 2Departamento de Biotecnologia Microbiana, Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma de Madrid Cantoblanco, 28049 Madrid, Spain 3Department of Molecular Biology, NCMLS M850/3.79 Geert Grooteplein 30, 6525 GA, Nijmegen, The Netherlands 4Laboratory of Microbiology, Wageningen University Hesselink van Suchtelenweg 4, 6307 CT Wageningen, The Netherlands

*To whom correspondence should be addressed. Tel: +44 (114) 222 2809; Fax: +44 (114) 222 2800; Email: j.rafferty{at}sheffield.ac.uk

Received November 21, 2005. Revised February 10, 2006. Accepted February 10, 2006.

The Lrp/AsnC family of transcriptional regulatory proteins is found in both archaea and bacteria. Members of the family influence cellular metabolism in both a global (Lrp) and specific (AsnC) manner, often in response to exogenous amino acid effectors. In the present study we have determined both the first bacterial and the highest resolution structures for members of the family. Escherichia coli AsnC is a specific gene regulator whose activity is triggered by asparagine binding. Bacillus subtilis LrpC is a global regulator involved in chromosome condensation. Our AsnC-asparagine structure is the first for a regulator–effector complex and is revealed as an octameric disc. Key ligand recognition residues are identified together with a route for ligand access. The LrpC structure reveals a stable octamer supportive of a topological role in dynamic DNA packaging. The structures yield significant clues to the functionality of Lrp/AsnC-type regulators with respect to ligand binding and oligomerization states as well as to their role in specific and global DNA regulation.


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