1d6k

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(New page: 200px<br /><applet load="1d6k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d6k" /> '''NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP...)
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'''NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX'''<br />
'''NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX'''<br />
==Overview==
==Overview==
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The structure of the complex between ribosomal protein L25 and a 37, nucleotide RNA molecule, which contains the E-loop and helix IV regions of, the E-domain of Escherichia coli 5S rRNA, has been determined to an, overall r.m.s. displacement of 1.08 A (backbone heavy atoms) by, heteronuclear NMR spectroscopy (Protein Databank code 1d6k). The, interacting molecular surfaces are bipartite for both the RNA and the, protein. One side of the six-stranded beta-barrel of L25 recognizes the, minor groove of the E-loop with very little change in the conformations of, either the protein or the RNA and with the RNA-protein interactions, occurring mainly along one strand of the E-loop duplex. This minor groove, recognition module includes two parallel beta-strands of L25, a hitherto, unknown RNA binding topology. Binding of the RNA also induces conversion, of a flexible loop to an alpha-helix in L25, the N-terminal tip of which, interacts with the widened major groove at the E-loop/helix IV junction of, the RNA. The structure of the complex reveals that the E-domain RNA serves, as a preformed docking partner, while the L25 protein has one preformed, and one induced recognition module.
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The structure of the complex between ribosomal protein L25 and a 37 nucleotide RNA molecule, which contains the E-loop and helix IV regions of the E-domain of Escherichia coli 5S rRNA, has been determined to an overall r.m.s. displacement of 1.08 A (backbone heavy atoms) by heteronuclear NMR spectroscopy (Protein Databank code 1d6k). The interacting molecular surfaces are bipartite for both the RNA and the protein. One side of the six-stranded beta-barrel of L25 recognizes the minor groove of the E-loop with very little change in the conformations of either the protein or the RNA and with the RNA-protein interactions occurring mainly along one strand of the E-loop duplex. This minor groove recognition module includes two parallel beta-strands of L25, a hitherto unknown RNA binding topology. Binding of the RNA also induces conversion of a flexible loop to an alpha-helix in L25, the N-terminal tip of which interacts with the widened major groove at the E-loop/helix IV junction of the RNA. The structure of the complex reveals that the E-domain RNA serves as a preformed docking partner, while the L25 protein has one preformed and one induced recognition module.
==About this Structure==
==About this Structure==
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1D6K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D6K OCA].
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1D6K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6K OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brown, L.R.]]
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[[Category: Brown, L R.]]
[[Category: Gorlach, M.]]
[[Category: Gorlach, M.]]
[[Category: Ohlenschlager, O.]]
[[Category: Ohlenschlager, O.]]
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[[Category: protein-rna complex]]
[[Category: protein-rna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:02:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:29 2008''

Revision as of 10:13, 21 February 2008


1d6k

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NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX

Overview

The structure of the complex between ribosomal protein L25 and a 37 nucleotide RNA molecule, which contains the E-loop and helix IV regions of the E-domain of Escherichia coli 5S rRNA, has been determined to an overall r.m.s. displacement of 1.08 A (backbone heavy atoms) by heteronuclear NMR spectroscopy (Protein Databank code 1d6k). The interacting molecular surfaces are bipartite for both the RNA and the protein. One side of the six-stranded beta-barrel of L25 recognizes the minor groove of the E-loop with very little change in the conformations of either the protein or the RNA and with the RNA-protein interactions occurring mainly along one strand of the E-loop duplex. This minor groove recognition module includes two parallel beta-strands of L25, a hitherto unknown RNA binding topology. Binding of the RNA also induces conversion of a flexible loop to an alpha-helix in L25, the N-terminal tip of which interacts with the widened major groove at the E-loop/helix IV junction of the RNA. The structure of the complex reveals that the E-domain RNA serves as a preformed docking partner, while the L25 protein has one preformed and one induced recognition module.

About this Structure

1D6K is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition., Stoldt M, Wohnert J, Ohlenschlager O, Gorlach M, Brown LR, EMBO J. 1999 Nov 15;18(22):6508-21. PMID:10562563

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