2dxi: Difference between revisions

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|PDB= 2dxi |SIZE=350|CAPTION= <scene name='initialview01'>2dxi</scene>, resolution 2.20&Aring;
|PDB= 2dxi |SIZE=350|CAPTION= <scene name='initialview01'>2dxi</scene>, resolution 2.20&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=GAU:(4S)-4-AMINO-5-HYDROXYPENTANOIC ACID'>GAU</scene>
|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=GAU:(4S)-4-AMINO-5-HYDROXYPENTANOIC+ACID'>GAU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
|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]  
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[2cuz|2CUZ]], [[2cv0|2CV0]], [[2cv1|2CV1]], [[2cv2|2CV2]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dxi OCA], [http://www.ebi.ac.uk/pdbsum/2dxi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dxi RCSB]</span>
}}
}}


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[[Category: Sekine, S.]]
[[Category: Sekine, S.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: ATP]]
[[Category: GAU]]
[[Category: MG]]
[[Category: ligase]]
[[Category: ligase]]
[[Category: national project on protein structural and functional analyse]]
[[Category: national project on protein structural and functional analyse]]
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[[Category: structural genomic]]
[[Category: structural genomic]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:58:16 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:40:59 2008''

Revision as of 23:40, 30 March 2008

File:2dxi.gif


Drag the structure with the mouse to rotate
2dxi, resolution 2.20Å
Ligands: A, ATP, C, G, GAU, MG, U
Activity: Glutamate--tRNA ligase, with EC number 6.1.1.17
Related: 2CUZ, 2CV0, 2CV1, 2CV2


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



2.2 A crystal structure of glutamyl-tRNA synthetase from Thermus thermophilus complexed with tRNA(Glu), ATP, and L-glutamol


Overview

Glutamyl-tRNA synthetase (GluRS) is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation. We analyzed the role of tRNA in amino acid recognition by crystallography. In the GluRS*tRNA(Glu)*Glu structure, GluRS and tRNA(Glu) collaborate to form a highly complementary L-glutamate-binding site. This collaborative site is functional, as it is formed in the same manner in pretransition-state mimic, GluRS*tRNA(Glu)*ATP*Eol (a glutamate analog), and posttransition-state mimic, GluRS*tRNA(Glu)*ESA (a glutamyl-adenylate analog) structures. In contrast, in the GluRS*Glu structure, only GluRS forms the amino acid-binding site, which is defective and accounts for the binding of incorrect amino acids, such as D-glutamate and L-glutamine. Therefore, tRNA(Glu) is essential for formation of the completely functional binding site for L-glutamate. These structures, together with our previously described structures, reveal that tRNA plays a crucial role in accurate positioning of both L-glutamate and ATP, thus driving the amino acid activation.

About this Structure

2DXI is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase., Sekine S, Shichiri M, Bernier S, Chenevert R, Lapointe J, Yokoyama S, Structure. 2006 Dec;14(12):1791-9. PMID:17161369

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