2ODR

Methanococcus Maripaludis Phosphoseryl-tRNA synthetase

2ODR の概要

• エントリーDOI: 10.2210/pdb2odr/pdb
• 分子名称: phosphoseryl-tRNA synthetase, ... (4 entities in total)
• 機能のキーワード: phosphoserine trna synthetase class ii, ligase
• 由来する生物種: Methanococcus maripaludis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 293734.87

構造登録者

Steitz, T.A.,Kamtekar, S. (登録日: 2006-12-26, 公開日: 2007-02-13, 最終更新日: 2023-12-27)

主引用文献

Kamtekar, S.,Hohn, M.J.,Park, H.S.,Schnitzbauer, M.,Sauerwald, A.,Soll, D.,Steitz, T.A.
Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase.
Proc.Natl.Acad.Sci.Usa, 104:2620-2625, 2007

PubMed Abstract: A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step pathway, first charging phosphoserine (Sep) onto tRNA(Cys) and subsequently converting it to Cys-tRNA(Cys). We have determined, at 3.2-A resolution, the structure of the Methanococcus maripaludis phosphoseryl-tRNA synthetase (SepRS), which catalyzes the first step of this pathway. The structure shows that SepRS is a class II, alpha(4) synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (alphabeta)(2) phenylalanyl-tRNA synthetase (PheRS). Homology modeling of a tRNA complex indicates that, in contrast to PheRS, a single monomer in the SepRS tetramer may recognize both the acceptor terminus and anticodon of a tRNA substrate. Using a complex with tungstate as a marker for the position of the phosphate moiety of Sep, we suggest that SepRS and PheRS bind their respective amino acid substrates in dissimilar orientations by using different residues.

PubMed: 17301225
DOI: 10.1073/pnas.0611504104

実験手法

X-RAY DIFFRACTION (3.228 Å)