Superposition of two tRNASer acceptor stem crystal structures: comparison of structure, ligands and hydration.
We solved the X-ray structures of two Escherichia coli tRNA(Ser) acceptor stem microhelices. As both tRNAs are aminoacylated by the same seryl-tRNA-synthetase, we performed a comparative structure analysis of both duplexes to investigate the helical conformation, the hydration patterns and magnesium binding sites. It is well accepted, that the hydration of RNA plays an important role in RNA-protein interactions and that the extensive solvent content of the minor groove has a special function in RNA. The detailed comparison of both tRNA(Ser) microhelices provides insights into the structural arrangement of the isoacceptor tRNA aminoacyl stems with respect to the surrounding water molecules and may eventually help us to understand their biological function at atomic resolution.
Eichert
André
A
Institute of Chemistry and Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin, Germany.
Fürste
Jens P
JP
Ulrich
Alexander
A
Betzel
Christian
C
Erdmann
Volker A
VA
Förster
Charlotte
C
D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism*; D008274:Magnesium / Q000737:chemistry; D009690:Nucleic Acid Conformation; D012362:RNA, Transfer, Ser / Q000737:chemistry*
D012362:RNA, Transfer, Ser; D008274:Magnesium