2f5t: Difference between revisions

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==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.

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==

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[[Category: Diederichs, K.]]

[[Category: Krug, M.]]

[[Category: Lee, S.J.]]

[[Category: Lee, S J.]]

[[Category: Welte, W.]]

[[Category: IMD]]

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[[Category: sugar-binding]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 16: / Line 16: @@
 [[Category: Diederichs, K.]]
 [[Category: Krug, M.]]
-[[Category: Lee, S.J.]]
+[[Category: Lee, S J.]]
 [[Category: Welte, W.]]
 [[Category: IMD]]
@@ Line 22: / Line 22: @@
 [[Category: sugar-binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:28:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:01 2008''