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J. Biol. Chem., Vol. 281, Issue 16, 10976-10982, April 21, 2006

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Crystal Structure of the Sugar Binding Domain of the Archaeal Transcriptional Regulator TrmB^*

From the Department of Biology, University of Konstanz, 78457 Konstanz, Germany

TrmB is an -glucoside-sensing transcriptional regulator controlling two operons encoding maltose/trehalose and maltodextrin ABC transporters of Pyrococcus furiosus. The crystal structure of an N-terminal truncated derivative of TrmB (amino acids 2-109 deleted; TrmB_2-109) was solved at 1.5 Å resolution. This protein has lost its DNA binding domain but has retained its sugar recognition site. The structure represents a novel sugar-binding fold. TrmB_2-109 bound maltose, glucose, sucrose, and maltotriose, exhibiting K_d values of 6.8, 25, 34, and 160 µM, respectively. TrmB_2-109 behaved as a monomer in dilute buffer solution in contrast to the full-length protein, which is a dimer. Co-crystallization with bound maltose identified a binding site involving seven amino acid residues: Ser²²⁹, Asn³⁰⁵, Gly³²⁰, Met³²¹, Val³²⁴, Ile³²⁵, and Glu³²⁶. Six of these residues interact with the nonreducing glucosyl residue of maltose. The nonreducing glucosyl residue is shared by all substrates bound to TrmB, suggesting it as a common recognition motif.

Received for publication, November 30, 2005 , and in revised form, February 9, 2006.

The atomic coordinates and structure factors (code 2F5T) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* 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.

¹ To whom correspondence should be addressed. Tel.: 49-7531-882206; Fax: 49-7531-883183; E-mail wolfram.welte{at}uni-konstanz.de.

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