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| {{STRUCTURE_2q7h| PDB=2q7h | SCENE= }} | | {{STRUCTURE_2q7h| PDB=2q7h | SCENE= }} |
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| '''Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphate'''
| | ===Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphate=== |
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| ==Overview==
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| Pyrrolysine (Pyl), the 22nd natural amino acid and genetically encoded by UAG, becomes attached to its cognate tRNA by pyrrolysyl-tRNA synthetase (PylRS). We have determined three crystal structures of the Methanosarcina mazei PylRS complexed with either AMP-PNP, Pyl-AMP plus pyrophosphate, or the Pyl analogue N-epsilon-[(cylopentyloxy)carbonyl]-L-lysine plus ATP. The structures reveal that PylRS utilizes a deep hydrophobic pocket for recognition of the Pyl side chain. A comparison of these structures with previously determined class II tRNA synthetase complexes illustrates that different substrate specificities derive from changes in a small number of residues that form the substrate side-chain-binding pocket. The knowledge of these structures allowed the placement of PylRS in the aminoacyl-tRNA synthetase (aaRS) tree as the last known synthetase that evolved for genetic code expansion, as well as the finding that Pyl arose before the last universal common ancestral state. The PylRS structure provides an excellent framework for designing new aaRSs with altered amino acid specificity.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17592110}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17592110 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17592110}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pyrrolysine]] | | [[Category: Pyrrolysine]] |
| [[Category: Pyrrolysyl-trna synthetase]] | | [[Category: Pyrrolysyl-trna synthetase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:28:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:14:35 2008'' |
