1o5t
From Proteopedia
(New page: 200px<br /> <applet load="1o5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o5t, resolution 2.50Å" /> '''Crystal structure o...) |
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caption="1o5t, resolution 2.50Å" /> | caption="1o5t, resolution 2.50Å" /> | ||
'''Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase'''<br /> | '''Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Tryptophan--tRNA_ligase Tryptophan--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.2 6.1.1.2] Full crystallographic information is available from [http:// | + | 1O5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Tryptophan--tRNA_ligase Tryptophan--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.2 6.1.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O5T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
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Revision as of 14:33, 15 February 2008
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Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase
Contents |
Overview
Human tryptophanyl-tRNA synthetase (hTrpRS) produces a full-length and, three N terminus-truncated forms through alternative splicing and, proteolysis. The shortest fragment that contains the aminoacylation, catalytic fragment (T2-hTrpRS) exhibits the most potent angiostatic, activity. We report here the crystal structure of T2-hTrpRS at 2.5 A, resolution, which was solved using the multi-wavelength anomalous, diffraction method. T2-hTrpRS shares a very low sequence homology of 22%, with Bacillus stearothermophilus TrpRS (bTrpRS); however, their overall, structures are strikingly similar. Structural comparison of T2-hTrpRS with, bTrpRS reveals substantial structural differences in the substrate-binding, pocket and at the entrance to the pocket that play important roles in, substrate binding and tRNA binding. T2-hTrpRS has a wide opening to the, active site and adopts a compact conformation similar to the closed, conformation of bTrpRS. These results suggest that mammalian and bacterial, TrpRSs might use different mechanisms to recognize the substrate. Modeling, studies indicate that tRNA binds with the dimeric enzyme and interacts, primarily with the connective polypeptide 1 of hTrpRS via its acceptor arm, and the alpha-helical domain of hTrpRS via its anticodon loop. Our results, also suggest that the angiostatic activity is likely located at the, alpha-helical domain, which resembles the short chain cytokines.
Disease
Known disease associated with this structure: Wolcott-Rallison syndrome OMIM:[604032]
About this Structure
1O5T is a Single protein structure of sequence from Homo sapiens. Active as Tryptophan--tRNA ligase, with EC number 6.1.1.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity., Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J, J Biol Chem. 2004 Feb 27;279(9):8378-88. Epub 2003 Dec 5. PMID:14660560
Page seeded by OCA on Fri Feb 15 16:33:11 2008
Categories: Homo sapiens | Single protein | Tryptophan--tRNA ligase | Arnold, E. | Ding, J. | Jia, J. | Jin, Y. | Liu, Y. | Shen, N. | Xu, X. | Yu, Y. | Four helix bundle | Rossmann fold
