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| {{STRUCTURE_1zh0| PDB=1zh0 | SCENE= }} | | {{STRUCTURE_1zh0| PDB=1zh0 | SCENE= }} |
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| '''Crystal Structure of L-3-(2-napthyl)alanine-tRNA synthetasein complex with L-3-(2-napthyl)alanine'''
| | ===Crystal Structure of L-3-(2-napthyl)alanine-tRNA synthetasein complex with L-3-(2-napthyl)alanine=== |
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| ==Overview==
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| Recently, tRNA aminoacyl-tRNA synthetase pairs have been evolved that allow one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic organisms. We have determined the crystal structures of two substrate-bound Methanococcus jannaschii tyrosyl aminoacyl-tRNA synthetases that charge the unnatural amino acids p-bromophenylalanine and 3-(2-naphthyl)alanine (NpAla). A comparison of these structures with the substrate-bound WT synthetase, as well as a mutant synthetase that charges p-acetylphenylalanine, shows that altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site. The high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases is rarely found in other mutant enzymes with altered specificities and provides an explanation for the surprising adaptability of the genetic code to novel amino acids.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16618920}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16618920 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16618920}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Trna synthetase]] | | [[Category: Trna synthetase]] |
| [[Category: Unnatural amino acid]] | | [[Category: Unnatural amino acid]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:36:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:28:18 2008'' |
