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Papers In Press, published online ahead of print June 1, 2005
Department of Biology, University of Konstanz, Konstanz 78457
Corresponding Author: andre.schiefner{at}uni-konstanz.de
Mlc from Escherichia coli is a transcriptional repressor controlling the expression of a number of genes encoding enzymes of the phospho-transferase system (PTS), including ptsG and manXYZ, the specific enzyme II for glucose and mannose PTS transporters. In addition, Mlc controls the transcription of malT, the gene of the global activator of the mal regulon. The inactivation of Mlc as a repressor is mediated by binding to an actively transporting PtsG (EIICBGlc). In this article we report the crystal structure of Mlc at 2.7 Å resolution representing the first described structure of a ROK (Repressors, Open reading frames and Kinases) family protein. Mlc forms stable dimers explaining its binding affinity to palindromic operator sites. The N-terminal helix-turn-helix domain of Mlc is stabilized by the amphipathic C-terminal helix implicated in EIICB{glc} binding earlier. Furthermore, the structure revealed a metal binding site within the cysteine-rich ROK consensus motif which coordinates a structurally important zinc ion. A strongly reduced repressor activity was observed when two of the zinc-coordinating cysteine residues were exchanged against serine or alanine, demonstrating the role of zinc in Mlc-mediated repressor function. The structures of a putative fructokinase from Bacillus subtilis, the glucokinase from Escherichia coli, and a glucomannokinase from Arthrobacter sp. showed high structural homology to the ROK family part of Mlc.
J. Biol. Chem, 10.1074/jbc.M504215200
Submitted on April 18, 2005
Revised on May 31, 2005
Accepted on June 1, 2005
The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli
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