3DSQ

Structure of Desulfitobacterium hafniense PylSc, a pyrrolysyl tRNA synthetase

Summary for 3DSQ

• Entry DOI: 10.2210/pdb3dsq/pdb
• Descriptor: Pyrrolysyl-tRNA synthetase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: homodimer, aminoacyl-trna synthetase, ligase
• Biological source: Desulfitobacterium hafniense (Desulfitobacterium frappieri)
• Total number of polymer chains: 2
• Total formula weight: 66679.04

Authors

Lee, M.M.,Chan, M.K. (deposition date: 2008-07-14, release date: 2008-08-12, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)