1ati
From Proteopedia
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| - | [[Image:1ati.jpg|left|200px]]<br /><applet load="1ati" size=" | + | [[Image:1ati.jpg|left|200px]]<br /><applet load="1ati" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ati, resolution 2.75Å" /> | caption="1ati, resolution 2.75Å" /> | ||
'''CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''<br /> | '''CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ATI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Glycine--tRNA_ligase Glycine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.14 6.1.1.14] Known structural/functional Site: <scene name='pdbsite=SA1:These Residues Are Found To Be Responsible For On The Ba ...'>SA1</scene>. Full crystallographic information is available from [http:// | + | 1ATI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Glycine--tRNA_ligase Glycine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.14 6.1.1.14] Known structural/functional Site: <scene name='pdbsite=SA1:These+Residues+Are+Found+To+Be+Responsible+For+On+The+Ba+...'>SA1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: synthetase]] | [[Category: synthetase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:31:34 2008'' |
Revision as of 07:31, 3 February 2008
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CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Overview
The sequence and crystal structure at 2.75 A resolution of the homodimeric, glycyl-tRNA synthetase from Thermus thermophilus, the first representative, of the last unknown class II synthetase subgroup, have been determined., The three class II synthetase sequence motifs are present but the, structure was essential for identification of motif 1, which does not, possess the proline previously believed to be an essential class II, invariant. Nevertheless, crucial contacts with the active site of the, other monomer involving motif 1 are conserved and a more comprehensive, description of class II now becomes possible. Each monomer consists of an, active site strongly resembling that of the aspartyl and seryl enzymes, a, C-terminal anticodon recognition domain of 100 residues and a third domain, unusually inserted between motifs 1 and 2 almost certainly interacting, with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel, five-stranded parallel-antiparallel beta-sheet structure with three, surrounding helices. The active site residues most probably responsible, for substrate recognition, in particular in the Gly binding pocket, can be, identified by inference from aspartyl-tRNA synthetase due to the conserved, nature of the class II active site.
About this Structure
1ATI is a Single protein structure of sequence from Thermus thermophilus. Active as Glycine--tRNA ligase, with EC number 6.1.1.14 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus., Logan DT, Mazauric MH, Kern D, Moras D, EMBO J. 1995 Sep 1;14(17):4156-67. PMID:7556056
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