2F5T

Crystal Structure of the sugar binding domain of the archaeal transcriptional regulator TrmB

Summary for 2F5T

• Entry DOI: 10.2210/pdb2f5t/pdb
• Related PRD ID: PRD_900001
• Descriptor: archaeal transcriptional regulator TrmB, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: sugar-binding, transcription
• Biological source: Thermococcus litoralis
• Total number of polymer chains: 1
• Total formula weight: 27050.77

Authors

Krug, M.,Lee, S.J.,Diederichs, K.,Boos, W.,Welte, W. (deposition date: 2005-11-27, release date: 2006-02-21, Last modification date: 2024-02-14)

Primary citation

Krug, M.,Lee, S.J.,Diederichs, K.,Boos, W.,Welte, W.
Crystal Structure of the Sugar Binding Domain of the Archaeal Transcriptional Regulator TrmB
J.Biol.Chem., 281:10976-10982, 2006

PubMed Abstract: 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 (amino acids 2-109 deleted; TrmB(delta2-109)) was solved at 1.5 A 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(delta2-109) bound maltose, glucose, sucrose, and maltotriose, exhibiting Kd values of 6.8, 25, 34, and 160 microM, respectively. TrmB(delta2-109) 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.

PubMed: 16473881
DOI: 10.1074/jbc.M512809200

Experimental method

X-RAY DIFFRACTION (1.45 Å)