2cky: Difference between revisions

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==Overview==

Riboswitches are untranslated regions of messenger RNA, which adopt, alternate structures depending on the binding of specific metabolites., Such conformational switching regulates the expression of proteins, involved in the biosynthesis of riboswitch substrates. Here, we present, the 2.9 angstrom-resolution crystal structure of the eukaryotic, Arabidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in, complex with its natural ligand. The riboswitch specifically recognizes, the TPP via conserved residues located within two highly distorted, parallel "sensor" helices. The structure provides the basis for, understanding the reorganization of the riboswitch fold upon TPP binding, and explains the mechanism of resistance to the antibiotic pyrithiamine.

Riboswitches are untranslated regions of messenger RNA, which adopt alternate structures depending on the binding of specific metabolites. Such conformational switching regulates the expression of proteins involved in the biosynthesis of riboswitch substrates. Here, we present the 2.9 angstrom-resolution crystal structure of the eukaryotic Arabidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in complex with its natural ligand. The riboswitch specifically recognizes the TPP via conserved residues located within two highly distorted parallel "sensor" helices. The structure provides the basis for understanding the reorganization of the riboswitch fold upon TPP binding and explains the mechanism of resistance to the antibiotic pyrithiamine.

==About this Structure==

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[[Category: nucleic acid]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Riboswitches are untranslated regions of messenger RNA, which adopt, alternate structures depending on the binding of specific metabolites., Such conformational switching regulates the expression of proteins, involved in the biosynthesis of riboswitch substrates. Here, we present, the 2.9 angstrom-resolution crystal structure of the eukaryotic, Arabidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in, complex with its natural ligand. The riboswitch specifically recognizes, the TPP via conserved residues located within two highly distorted, parallel "sensor" helices. The structure provides the basis for, understanding the reorganization of the riboswitch fold upon TPP binding, and explains the mechanism of resistance to the antibiotic pyrithiamine.
+Riboswitches are untranslated regions of messenger RNA, which adopt alternate structures depending on the binding of specific metabolites. Such conformational switching regulates the expression of proteins involved in the biosynthesis of riboswitch substrates. Here, we present the 2.9 angstrom-resolution crystal structure of the eukaryotic Arabidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in complex with its natural ligand. The riboswitch specifically recognizes the TPP via conserved residues located within two highly distorted parallel "sensor" helices. The structure provides the basis for understanding the reorganization of the riboswitch fold upon TPP binding and explains the mechanism of resistance to the antibiotic pyrithiamine.
 ==About this Structure==
@@ Line 20: / Line 20: @@
 [[Category: nucleic acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:36:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:44 2008''