L. Jovine et al., The crystal structure of yeast phenylalanine tRNA at 2.0 angstrom resolution: Cleavage by Mg2+ in 15-year old crystals, J MOL BIOL, 301(2), 2000, pp. 401-414
We have re-determined the crystal structure of yeast tRNA(Phe) to 2.0 Angst
rom resolution using 15 year old crystals. The accuracy of the new structur
e, due both to higher resolution data and formerly unavailable refinement m
ethods, consolidates the previous structural information, but also reveals
novel details. Ln particular, the water structure around the tightly bound
Mg2+ is now clearly resolved, and hence provides more accurate information
on the geometry of the magnesium-binding sites and the role of water molecu
les in coordinating the metal ions to the tRNA. We have assigned a total of
ten magnesium ions and identified a partly conserved geometry for high-aff
inity Mg2+ binding. In the electron density map there is also clear density
for a spermine molecule binding in the major groove of the T Psi C arm and
also contacting a symmetry-related tRNA molecule. Interestingly, we have a
lso found that two specific regions of the tRNA in the crystals are partial
ly cleaved. The sites of hydrolysis are within the D and anticodon loops in
the vicinity of Mg2+. (C) 2000 Academic Press.