1n78

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==Reference==
==Reference==
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ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding., Sekine S, Nureki O, Dubois DY, Bernier S, Chenevert R, Lapointe J, Vassylyev DG, Yokoyama S, EMBO J. 2003 Feb 3;22(3):676-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12554668 12554668]
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<ref group="xtra">PMID:12554668</ref><references group="xtra"/>
[[Category: Glutamate--tRNA ligase]]
[[Category: Glutamate--tRNA ligase]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 14:05:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:46:23 2009''

Revision as of 14:46, 17 February 2009

Image:1n78.png

Template:STRUCTURE 1n78

Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(Glu) and glutamol-AMP.

Template:ABSTRACT PUBMED 12554668

About this Structure

1N78 is a 4 chains structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

  • Sekine S, Nureki O, Dubois DY, Bernier S, Chenevert R, Lapointe J, Vassylyev DG, Yokoyama S. ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. EMBO J. 2003 Feb 3;22(3):676-88. PMID:12554668 doi:http://dx.doi.org/10.1093/emboj/cdg053

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