2f5t
From Proteopedia
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Crystal Structure of the sugar binding domain of the archaeal transcriptional regulator TrmB
Overview
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.
About this Structure
2F5T is a Single protein structure of sequence from Thermococcus litoralis with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the sugar binding domain of the archaeal transcriptional regulator TrmB., Krug M, Lee SJ, Diederichs K, Boos W, Welte W, J Biol Chem. 2006 Apr 21;281(16):10976-82. Epub 2006 Feb 10. PMID:16473881
Page seeded by OCA on Thu Feb 21 17:18:01 2008
Categories: Single protein | Thermococcus litoralis | Boos, W. | Diederichs, K. | Krug, M. | Lee, S J. | Welte, W. | IMD | MAL | Sugar-binding
