2ODR

Methanococcus Maripaludis Phosphoseryl-tRNA synthetase

Summary for 2ODR

• Entry DOI: 10.2210/pdb2odr/pdb
• Descriptor: phosphoseryl-tRNA synthetase, ... (4 entities in total)
• Functional Keywords: phosphoserine trna synthetase class ii, ligase
• Biological source: Methanococcus maripaludis; More
• Total number of polymer chains: 4
• Total formula weight: 293734.87

Authors

Steitz, T.A.,Kamtekar, S. (deposition date: 2006-12-26, release date: 2007-02-13, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.228 Å)