1r6t
From Proteopedia
(New page: 200px<br /> <applet load="1r6t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6t, resolution 2.10Å" /> '''crystal structure o...) |
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caption="1r6t, resolution 2.10Å" /> | caption="1r6t, resolution 2.10Å" /> | ||
'''crystal structure of human tryptophanyl-tRNA synthetase'''<br /> | '''crystal structure of human tryptophanyl-tRNA synthetase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with TYM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1R6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=TYM:'>TYM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1R6T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rossmann fold catalytical domain]] | [[Category: rossmann fold catalytical domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:47:12 2008'' |
Revision as of 14:47, 15 February 2008
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crystal structure of human tryptophanyl-tRNA synthetase
Contents |
Overview
Early forms of the genetic code likely generated "statistical" proteins, with similar side chains occupying the same sequence positions at, different ratios. In this scenario, groups of related side chains were, treated by aminoacyl-tRNA synthetases as a single molecular species until, a discrimination mechanism developed that could separate them. The, aromatic amino acids tryptophan, tyrosine, and phenylalanine likely, constituted one of these groups. A crystal structure of human, tryptophanyl-tRNA synthetase was solved at 2.1 A with a, tryptophanyl-adenylate bound at the active site. A cocrystal structure of, an active fragment of human tyrosyl-tRNA synthetase with its cognate amino, acid analog was also solved at 1.6 A. The two structures enabled active, site identifications and provided the information for structure-based, sequence alignments of approximately 45 orthologs of each enzyme. Two, critical positions shared by all tyrosyl-tRNA synthetases and, tryptophanyl-tRNA synthetases for amino acid discrimination were, identified. The variations at these two positions and phylogenetic, analyses based on the structural information suggest that, in contrast to, many other amino acids, discrimination of tyrosine from tryptophan, occurred late in the development of the genetic code.
Disease
Known disease associated with this structure: Wolcott-Rallison syndrome OMIM:[604032]
About this Structure
1R6T is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Tryptophan--tRNA ligase, with EC number 6.1.1.2 Full crystallographic information is available from OCA.
Reference
Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains., Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L, Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15376-80. Epub 2003 Dec 11. PMID:14671330
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