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| {{STRUCTURE_2f5t| PDB=2f5t | SCENE= }} | | {{STRUCTURE_2f5t| PDB=2f5t | SCENE= }} |
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| '''Crystal Structure of the sugar binding domain of the archaeal transcriptional regulator TrmB'''
| | ===Crystal Structure of the sugar binding domain of the archaeal transcriptional regulator TrmB=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16473881}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16473881 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16473881}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Welte, W.]] | | [[Category: Welte, W.]] |
| [[Category: Sugar-binding]] | | [[Category: Sugar-binding]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:29:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:14:24 2008'' |
