1kos

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(New page: 200px<br /><applet load="1kos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kos" /> '''SOLUTION NMR STRUCTURE OF AN ANALOG OF THE Y...)
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'''SOLUTION NMR STRUCTURE OF AN ANALOG OF THE YEAST TRNA PHE T STEM LOOP CONTAINING RIBOTHYMIDINE AT ITS NATURALLY OCCURRING POSITION'''<br />
'''SOLUTION NMR STRUCTURE OF AN ANALOG OF THE YEAST TRNA PHE T STEM LOOP CONTAINING RIBOTHYMIDINE AT ITS NATURALLY OCCURRING POSITION'''<br />
==Overview==
==Overview==
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The structure of an analogue of the yeast tRNAPhe T Psi C stem-loop has, been determined by NMR spectroscopy and restrained molecular dynamics. The, molecule contained the highly conserved modification ribothymidine at its, naturally occurring position. The ribothymidine-modified T Psi C stem-loop, is the product of the m5U54-tRNA methyltransferase, but is not a substrate, for the m1A58-tRNA methyltransferase. Site-specific substitutions and 15N, labels were used to confirm the assignment of NOESY cross-peaks critical, in defining the global fold of the molecule. The structure is unusual in, that the loop folds far over into the major groove of the curved stem., This conformation is stabilized by both stacking interactions and hydrogen, bond formation. Furthermore, this conformation appears to be unique among, RNA hairpins of similar size. There is, however, a considerable, resemblance to the analogous domain in the crystal structure of the, full-length yeast tRNAPhe. We believe, therefore, that the structure we, have determined may represent an intermediate in the folding pathway, during the maturation of tRNA.
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The structure of an analogue of the yeast tRNAPhe T Psi C stem-loop has been determined by NMR spectroscopy and restrained molecular dynamics. The molecule contained the highly conserved modification ribothymidine at its naturally occurring position. The ribothymidine-modified T Psi C stem-loop is the product of the m5U54-tRNA methyltransferase, but is not a substrate for the m1A58-tRNA methyltransferase. Site-specific substitutions and 15N labels were used to confirm the assignment of NOESY cross-peaks critical in defining the global fold of the molecule. The structure is unusual in that the loop folds far over into the major groove of the curved stem. This conformation is stabilized by both stacking interactions and hydrogen bond formation. Furthermore, this conformation appears to be unique among RNA hairpins of similar size. There is, however, a considerable resemblance to the analogous domain in the crystal structure of the full-length yeast tRNAPhe. We believe, therefore, that the structure we have determined may represent an intermediate in the folding pathway during the maturation of tRNA.
==About this Structure==
==About this Structure==
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1KOS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KOS OCA].
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1KOS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOS OCA].
==Reference==
==Reference==
A distinctive RNA fold: the solution structure of an analogue of the yeast tRNAPhe T Psi C domain., Koshlap KM, Guenther R, Sochacka E, Malkiewicz A, Agris PF, Biochemistry. 1999 Jul 6;38(27):8647-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10393540 10393540]
A distinctive RNA fold: the solution structure of an analogue of the yeast tRNAPhe T Psi C domain., Koshlap KM, Guenther R, Sochacka E, Malkiewicz A, Agris PF, Biochemistry. 1999 Jul 6;38(27):8647-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10393540 10393540]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Agris, P.F.]]
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[[Category: Agris, P F.]]
[[Category: Guenther, R.]]
[[Category: Guenther, R.]]
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[[Category: Koshlap, K.M.]]
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[[Category: Koshlap, K M.]]
[[Category: Malkiewicz, A.]]
[[Category: Malkiewicz, A.]]
[[Category: Sochacka, E.]]
[[Category: Sochacka, E.]]
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[[Category: trna domain]]
[[Category: trna domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:41:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:22 2008''

Revision as of 11:36, 21 February 2008


1kos

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SOLUTION NMR STRUCTURE OF AN ANALOG OF THE YEAST TRNA PHE T STEM LOOP CONTAINING RIBOTHYMIDINE AT ITS NATURALLY OCCURRING POSITION

Overview

The structure of an analogue of the yeast tRNAPhe T Psi C stem-loop has been determined by NMR spectroscopy and restrained molecular dynamics. The molecule contained the highly conserved modification ribothymidine at its naturally occurring position. The ribothymidine-modified T Psi C stem-loop is the product of the m5U54-tRNA methyltransferase, but is not a substrate for the m1A58-tRNA methyltransferase. Site-specific substitutions and 15N labels were used to confirm the assignment of NOESY cross-peaks critical in defining the global fold of the molecule. The structure is unusual in that the loop folds far over into the major groove of the curved stem. This conformation is stabilized by both stacking interactions and hydrogen bond formation. Furthermore, this conformation appears to be unique among RNA hairpins of similar size. There is, however, a considerable resemblance to the analogous domain in the crystal structure of the full-length yeast tRNAPhe. We believe, therefore, that the structure we have determined may represent an intermediate in the folding pathway during the maturation of tRNA.

About this Structure

1KOS is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

A distinctive RNA fold: the solution structure of an analogue of the yeast tRNAPhe T Psi C domain., Koshlap KM, Guenther R, Sochacka E, Malkiewicz A, Agris PF, Biochemistry. 1999 Jul 6;38(27):8647-56. PMID:10393540

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