3DSQ

Structure of Desulfitobacterium hafniense PylSc, a pyrrolysyl tRNA synthetase

3DSQ の概要

• エントリーDOI: 10.2210/pdb3dsq/pdb
• 分子名称: Pyrrolysyl-tRNA synthetase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: homodimer, aminoacyl-trna synthetase, ligase
• 由来する生物種: Desulfitobacterium hafniense (Desulfitobacterium frappieri)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66679.04

構造登録者

Lee, M.M.,Chan, M.K. (登録日: 2008-07-14, 公開日: 2008-08-12, 最終更新日: 2023-08-30)

主引用文献

Lee, M.M.,Jiang, R.,Jain, R.,Larue, R.C.,Krzycki, J.,Chan, M.K.
Structure of Desulfitobacterium hafniense PylSc, a pyrrolysyl-tRNA synthetase.
Biochem.Biophys.Res.Commun., 374:470-474, 2008

PubMed Abstract: Pyrrolysine, the 22nd genetically-encoded amino acid, is charged onto its specific tRNA by PylS, a pyrrolysyl-tRNA synthetase. While PylS is found as a single protein in certain archaeal methanogens, in the gram-positive bacterium Desulfitobacterium hafniense, PylS is divided into two separate proteins, PylSn and PylSc, corresponding to the N-terminal and C-terminal domains of the single PylS protein found in methanogens. Previous crystallographic studies have provided the structure of a truncated C-terminal portion of the archaeal Methanosarcina mazei PylS associated with catalysis. Here, we report the apo 2.1A resolution structure of the intact D. hafniense PylSc protein and compare it to structures of the C-terminal truncated PylS from methanogenic species. In PylSc, the hydrophobic pocket binding the ring of pyrrolysine is more constrained than in the archaeal enzyme; other structural differences are also apparent.

PubMed: 18656445
DOI: 10.1016/j.bbrc.2008.07.074

実験手法

X-RAY DIFFRACTION (2.1 Å)