1mms

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(New page: 200px<br /><applet load="1mms" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mms, resolution 2.57&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1mms.gif|left|200px]]<br /><applet load="1mms" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mms, resolution 2.57&Aring;" />
caption="1mms, resolution 2.57&Aring;" />
'''CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN L11-RNA COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN L11-RNA COMPLEX'''<br />
==Overview==
==Overview==
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We report the crystal structure of a 58 nucleotide fragment of 23S, ribosomal RNA bound to ribosomal protein L11. This highly conserved, ribonucleoprotein domain is the target for the thiostrepton family of, antibiotics that disrupt elongation factor function. The highly compact, RNA has both familiar and novel structural motifs. While the C-terminal, domain of L11 binds RNA tightly, the N-terminal domain makes only limited, contacts with RNA and is proposed to function as a switch that reversibly, associates with an adjacent region of RNA. The sites of mutations, conferring resistance to thiostrepton and micrococcin line a narrow cleft, between the RNA and the N-terminal domain. These antibiotics are proposed, to bind in this cleft, locking the putative switch and interfering with, the function of elongation factors.
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We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors.
==About this Structure==
==About this Structure==
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1MMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with CD, MG and MMC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MMS OCA].
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1MMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=MMC:'>MMC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMS OCA].
==Reference==
==Reference==
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Guymon, R.]]
[[Category: Guymon, R.]]
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[[Category: Mccutcheon, J.P.]]
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[[Category: Mccutcheon, J P.]]
[[Category: Ramakrishnan, V.]]
[[Category: Ramakrishnan, V.]]
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[[Category: White, S.W.]]
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[[Category: White, S W.]]
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[[Category: Wimberly, B.T.]]
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[[Category: Wimberly, B T.]]
[[Category: CD]]
[[Category: CD]]
[[Category: MG]]
[[Category: MG]]
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[[Category: translocation]]
[[Category: translocation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:32:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:46 2008''

Revision as of 11:56, 21 February 2008


1mms, resolution 2.57Å

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CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN L11-RNA COMPLEX

Overview

We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors.

About this Structure

1MMS is a Single protein structure of sequence from Thermotoga maritima with , and as ligands. Full crystallographic information is available from OCA.

Reference

A detailed view of a ribosomal active site: the structure of the L11-RNA complex., Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V, Cell. 1999 May 14;97(4):491-502. PMID:10338213

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