1exd

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(New page: 200px<br /><applet load="1exd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1exd, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1exd.gif|left|200px]]<br /><applet load="1exd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1exd, resolution 2.70&Aring;" />
caption="1exd, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF A TIGHT-BINDING GLUTAMINE TRNA BOUND TO GLUTAMINE AMINOACYL TRNA SYNTHETASE'''<br />
'''CRYSTAL STRUCTURE OF A TIGHT-BINDING GLUTAMINE TRNA BOUND TO GLUTAMINE AMINOACYL TRNA SYNTHETASE'''<br />
==Overview==
==Overview==
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Guided by an in vitro selection experiment designed to obtain tight, binding aptamers of Escherichia coli glutamine specific tRNA (tRNAGln) for, glutaminyl-tRNA synthetase (GlnRS), we have engineered a tRNA mutant in, which the five-nucleotide variable loop sequence 5'-44CAUUC48-3' is, replaced by 5'-44AGGU48-3'. This mutant tRNA binds to GlnRS with 30-fold, improved affinity compared to the wild type. The 2.7 A cocrystal structure, of the RNA aptamer-GlnRS complex reveals major rearrangements in the, central tertiary core of the tRNA, while maintaining an RNA-protein, interface identical to the wild type. The repacked RNA core features a, novel hydrogen bonding arrangement of the trans Levitt pair G15-U48, a new, sulfate binding pocket in the major groove, and increased hydrophobic, stacking interactions among the bases. These data suggest that enhanced, protein binding to a mutant globular RNA can arise from stabilization of, RNA tertiary interactions rather than optimization of RNA-protein, contacts.
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Guided by an in vitro selection experiment designed to obtain tight binding aptamers of Escherichia coli glutamine specific tRNA (tRNAGln) for glutaminyl-tRNA synthetase (GlnRS), we have engineered a tRNA mutant in which the five-nucleotide variable loop sequence 5'-44CAUUC48-3' is replaced by 5'-44AGGU48-3'. This mutant tRNA binds to GlnRS with 30-fold improved affinity compared to the wild type. The 2.7 A cocrystal structure of the RNA aptamer-GlnRS complex reveals major rearrangements in the central tertiary core of the tRNA, while maintaining an RNA-protein interface identical to the wild type. The repacked RNA core features a novel hydrogen bonding arrangement of the trans Levitt pair G15-U48, a new sulfate binding pocket in the major groove, and increased hydrophobic stacking interactions among the bases. These data suggest that enhanced protein binding to a mutant globular RNA can arise from stabilization of RNA tertiary interactions rather than optimization of RNA-protein contacts.
==About this Structure==
==About this Structure==
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1EXD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and A as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXD OCA].
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1EXD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=A:'>A</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXD OCA].
==Reference==
==Reference==
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[[Category: Glutamine--tRNA ligase]]
[[Category: Glutamine--tRNA ligase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bullock, T.L.]]
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[[Category: Bullock, T L.]]
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[[Category: Perona, J.J.]]
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[[Category: Perona, J J.]]
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[[Category: Sherlin, L.D.]]
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[[Category: Sherlin, L D.]]
[[Category: A]]
[[Category: A]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: trna-protein complex]]
[[Category: trna-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:23:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:31 2008''

Revision as of 10:32, 21 February 2008


1exd, resolution 2.70Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF A TIGHT-BINDING GLUTAMINE TRNA BOUND TO GLUTAMINE AMINOACYL TRNA SYNTHETASE

Overview

Guided by an in vitro selection experiment designed to obtain tight binding aptamers of Escherichia coli glutamine specific tRNA (tRNAGln) for glutaminyl-tRNA synthetase (GlnRS), we have engineered a tRNA mutant in which the five-nucleotide variable loop sequence 5'-44CAUUC48-3' is replaced by 5'-44AGGU48-3'. This mutant tRNA binds to GlnRS with 30-fold improved affinity compared to the wild type. The 2.7 A cocrystal structure of the RNA aptamer-GlnRS complex reveals major rearrangements in the central tertiary core of the tRNA, while maintaining an RNA-protein interface identical to the wild type. The repacked RNA core features a novel hydrogen bonding arrangement of the trans Levitt pair G15-U48, a new sulfate binding pocket in the major groove, and increased hydrophobic stacking interactions among the bases. These data suggest that enhanced protein binding to a mutant globular RNA can arise from stabilization of RNA tertiary interactions rather than optimization of RNA-protein contacts.

About this Structure

1EXD is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Glutamine--tRNA ligase, with EC number 6.1.1.18 Full crystallographic information is available from OCA.

Reference

Tertiary core rearrangements in a tight binding transfer RNA aptamer., Bullock TL, Sherlin LD, Perona JJ, Nat Struct Biol. 2000 Jun;7(6):497-504. PMID:10881199

Page seeded by OCA on Thu Feb 21 12:32:31 2008

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