1q11: Difference between revisions
New page: left|200px<br /> <applet load="1q11" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q11, resolution 1.6Å" /> '''Crystal structure of... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1q11.gif|left|200px]]<br /> | [[Image:1q11.gif|left|200px]]<br /><applet load="1q11" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1q11" size=" | |||
caption="1q11, resolution 1.6Å" /> | caption="1q11, resolution 1.6Å" /> | ||
'''Crystal structure of an active fragment of human tyrosyl-tRNA synthetase with tyrosinol'''<br /> | '''Crystal structure of an active fragment of human tyrosyl-tRNA synthetase with tyrosinol'''<br /> | ||
==Overview== | ==Overview== | ||
Early forms of the genetic code likely generated "statistical" proteins, with similar side chains occupying the same sequence positions at | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1Q11 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 PO4, K, TYB and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http:// | 1Q11 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=PO4:'>PO4</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=TYB:'>TYB</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q11 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tyrosine--tRNA ligase]] | [[Category: Tyrosine--tRNA ligase]] | ||
[[Category: Pouplana, L | [[Category: Pouplana, L Ribas de.]] | ||
[[Category: Schimmel, P.]] | [[Category: Schimmel, P.]] | ||
[[Category: Yang, X | [[Category: Yang, X L.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: K]] | [[Category: K]] | ||
| Line 29: | Line 28: | ||
[[Category: substrate analog tyrosinol co-crystalized]] | [[Category: substrate analog tyrosinol co-crystalized]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:42 2008'' | ||
Revision as of 15:34, 21 February 2008
|
Crystal structure of an active fragment of human tyrosyl-tRNA synthetase with tyrosinol
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Charcot-Marie-Tooth disease, dominant intermediate C OMIM:[603623]
About this StructureAbout this Structure
1Q11 is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Tyrosine--tRNA ligase, with EC number 6.1.1.1 Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 14:34:42 2008