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2cfo

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[[Image:2cfo.gif|left|200px]]<br /><applet load="2cfo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cfo.gif|left|200px]]
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caption="2cfo, resolution 2.45&Aring;" />
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'''NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU'''<br />
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{{Structure
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|PDB= 2cfo |SIZE=350|CAPTION= <scene name='initialview01'>2cfo</scene>, resolution 2.45&Aring;
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|SITE= <scene name='pdbsite=AC1:GLU+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GLU:GLUTAMIC ACID'>GLU</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17]
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|GENE=
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}}
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'''NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CFO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus] with <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] Known structural/functional Site: <scene name='pdbsite=AC1:GLU+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFO OCA].
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2CFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFO OCA].
==Reference==
==Reference==
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Crystal structure of a non-discriminating glutamyl-tRNA synthetase., Schulze JO, Masoumi A, Nickel D, Jahn M, Jahn D, Schubert WD, Heinz DW, J Mol Biol. 2006 Sep 1;361(5):888-97. Epub 2006 Jul 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16876193 16876193]
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Crystal structure of a non-discriminating glutamyl-tRNA synthetase., Schulze JO, Masoumi A, Nickel D, Jahn M, Jahn D, Schubert WD, Heinz DW, J Mol Biol. 2006 Sep 1;361(5):888-97. Epub 2006 Jul 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16876193 16876193]
[[Category: Glutamate--tRNA ligase]]
[[Category: Glutamate--tRNA ligase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein biosynthesis]]
[[Category: protein biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:48 2008''

Revision as of 14:14, 20 March 2008


PDB ID 2cfo

Drag the structure with the mouse to rotate
, resolution 2.45Å
Sites:
Ligands:
Activity: Glutamate--tRNA ligase, with EC number 6.1.1.17
Coordinates: save as pdb, mmCIF, xml



NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU


Overview

Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA(Gln) is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA(Glu) and tRNA(Gln) with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA(Glu). Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS(Tel)) in complex with glutamate at a resolution of 2.45 A. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS(Tth)). We confirm experimentally that GluRS(Tel) is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA(Glu) and of Glu-tRNA(Gln). Anticodons of tRNA(Glu) (34C/UUC36) and tRNA(Gln) (34C/UUG36) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS(Tth) by the residue Arg358. In ND-GluRS(Tel) this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA(Gln) to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.

About this Structure

2CFO is a Single protein structure of sequence from Synechococcus elongatus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a non-discriminating glutamyl-tRNA synthetase., Schulze JO, Masoumi A, Nickel D, Jahn M, Jahn D, Schubert WD, Heinz DW, J Mol Biol. 2006 Sep 1;361(5):888-97. Epub 2006 Jul 5. PMID:16876193

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