2Q7E

The structure of pyrrolysyl-tRNA synthetase bound to an ATP analogue

2Q7E の概要

• エントリーDOI: 10.2210/pdb2q7e/pdb
• 関連するPDBエントリー: 2q7g 2q7h
• 分子名称: Pyrrolysyl-tRNA synthetase, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, pyrrolysine, ligase
• 由来する生物種: Methanosarcina mazei
• 細胞内の位置: Cytoplasm (By similarity): Q8PWY1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34653.78

構造登録者

Kavran, J.M.,Steitz, T.A. (登録日: 2007-06-06, 公開日: 2007-07-24, 最終更新日: 2024-02-21)

主引用文献

Kavran, J.M.,Gundllapalli, S.,O'donoghue, P.,Englert, M.,Soll, D.,Steitz, T.A.
Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation.
Proc.Natl.Acad.Sci.Usa, 104:11268-11273, 2007

PubMed Abstract: 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.

PubMed: 17592110
DOI: 10.1073/pnas.0704769104

実験手法

X-RAY DIFFRACTION (1.8 Å)