Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB

TrmB is an alpha-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 was solved at 1.5A 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 bound maltose, glucose, sucrose, and maltotriose, exhibiting Kd values of 6.8, 25, 34, and 160 μM, respectively. TrmB 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.

Subject (DDC)

570 Biosciences, Biology

Cite This

ISO 690

KRUG, Michael, Sung-Jae LEE, Kay DIEDERICHS, Winfried BOOS, Wolfram WELTE, 2006. Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB. In: Journal of Biological Chemistry. 281(16), pp. 10976-10982. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M512809200

BibTex

@article{Krug2006Cryst-7898,
  year={2006},
  doi={10.1074/jbc.M512809200},
  title={Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB},
  number={16},
  volume={281},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={10976--10982},
  author={Krug, Michael and Lee, Sung-Jae and Diederichs, Kay and Boos, Winfried and Welte, Wolfram}
}

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    <dcterms:abstract xml:lang="eng">TrmB is an alpha-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 was solved at 1.5A 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 bound maltose, glucose, sucrose, and maltotriose, exhibiting Kd values of 6.8, 25, 34, and 160 μM, respectively. TrmB 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.</dcterms:abstract>
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