Superposition of a tRNASer acceptor stem microhelix into the seryl-tRNA synthetase complex.
Aminoacyl-tRNA synthetases catalyze the formation of aminoacyl-tRNAs. Seryl-tRNA synthetase is a class II synthetase, which depends on rather few and simple identity elements in tRNA(Ser) to determine the amino acid specificity. tRNA(Ser) acceptor stem microhelices can be aminoacylated with serine, which makes this part of the tRNA a valuable tool for investigating the structural motifs in a tRNA(Ser)-seryl-tRNA synthetase complex. A 1.8A-resolution tRNA(Ser) acceptor stem crystal structure was superimposed to a 2.9A-resolution crystal structure of a tRNA(Ser)-seryl-tRNA synthetase complex for a visualization of the binding environment of the tRNA(Ser) microhelix.
Förster
C
C
Institute of Chemistry and Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin, Germany.
Brauer
A B E
AB
Fürste
J P
JP
Betzel
Ch
Ch
Weber
M
M
Cordes
F
F
Erdmann
V A
VA
D000926:Anticodon / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism; D012362:RNA, Transfer, Ser / Q000737:chemistry* / Q000378:metabolism; D012714:Serine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism
D000926:Anticodon; D012346:RNA, Transfer, Amino Acyl; D012362:RNA, Transfer, Ser; D012714:Serine-tRNA Ligase