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J. Biol. Chem., Vol. 282, Issue 19, 14655-14664, May 11, 2007

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The Structure and Transcriptional Analysis of a Global Regulator from Neisseria meningitidis^*

Jingshan Ren, Sarah Sainsbury, Susan E. Combs^¶, Richard G. Capper^¶, Philip W. Jordan^¶, Nick S. Berrow, David K. Stammers, Nigel J. Saunders^¶, and Raymond J. Owens¹

From the Oxford Protein Production Facility and Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN and the ^¶Bacterial Pathogenesis and Functional Genomics Group, Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom

Neisseria meningitidis, a causative agent of bacterial meningitis, has a relatively small repertoire of transcription factors, including NMB0573 (annotated AsnC), a member of the Lrp-AsnC family of regulators that are widely expressed in both Bacteria and Archaea. In the present study we show that NMB0573 binds to L-leucine and L-methionine and have solved the structure of the protein with and without bound amino acids. This has shown, for the first time that amino acid binding does not induce significant conformational changes in the structure of an AsnC/Lrp regulator although it does appear to stabilize the octameric assembly of the protein. Transcriptional profiling of wild-type and NMB0573 knock-out strains of N. meningitidis has shown that NMB0573 is associated with an adaptive response to nutrient poor conditions reflected in a reduction in major surface protein expression. On the basis of its structure and the transcriptional response, we propose that NMB0573 is a global regulator in Neisseria controlling responses to nutrient availability through indicators of general amino acid abundance: leucine and methionine.

Received for publication, February 5, 2007 , and in revised form, March 19, 2007.

The atomic coordinates and structure factors (code 2P5V, 2P6S, and 2P6T) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Medical Research Council, UK. The Oxford Protein Production Facility is part of the Structural Proteomics in Europe (SPINE) consortium supported by European Commission Grant QLG2-CT-2002-00988. The microarray facilities were largely funded with support from the EPA Cephalosporin Trust and BASE and microarray analysis was supported by the Dunn School/WIMM Computational Biology Research Group. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S1.

¹ To whom correspondence should be addressed. Tel.: 44-0-1865-287748; Fax: 44-0-1865-287547; E-mail: ray{at}strubi.ox.ac.uk.

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