1SER

THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER

Summary for 1SER

• Entry DOI: 10.2210/pdb1ser/pdb
• Descriptor: TRNASER, PROTEIN (SERYL-TRNA SYNTHETASE (E.C.6.1.1.11)) (3 entities in total)
• Functional Keywords: protein-t-rna complex, ligase-rna complex, ligase/rna
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm : P34945
• Total number of polymer chains: 3
• Total formula weight: 126144.78

Authors

Biou, S.,Cusack, V.,Yaremchuk, A.,Tukalo, M. (deposition date: 1994-02-21, release date: 1994-04-30, Last modification date: 2024-02-14)

Primary citation

Biou, V.,Yaremchuk, A.,Tukalo, M.,Cusack, S.
The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser).
Science, 263:1404-1410, 1994

PubMed Abstract: The crystal structure of Thermus thermophilus seryl-transfer RNA synthetase, a class 2 aminoacyl-tRNA synthetase, complexed with a single tRNA(Ser) molecule was solved at 2.9 A resolution. The structure revealed how insertion of conserved base G20b from the D loop into the core of the tRNA determines the orientation of the long variable arm, which is a characteristic feature of most serine specific tRNAs. On tRNA binding, the antiparallel coiled-coil domain of one subunit of the synthetase makes contacts with the variable arm and T psi C loop of the tRNA and directs the acceptor stem of the tRNA into the active site of the other subunit. Specificity depends principally on recognition of the shape of tRNA(Ser) through backbone contacts and secondarily on sequence specific interactions.

PubMed: 8128220

Experimental method

X-RAY DIFFRACTION (2.9 Å)