International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

© International Union of Crystallography 2006
International Tables for Crystallography (2006). Vol. F. ch. 23.2, pp. 583-584   | 1 | 2 |

Section 23.2.4.4. Transfer RNA

A. E. Hodela‡ and F. A. Quiochob

aDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA, and  bHoward Hughes Medical Institute and Department of Biochemistry, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA

23.2.4.4. Transfer RNA

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In the four known structures of tRNA bound to their aminoacyl tRNA synthetases (Cusack et al., 1996a[link],b[link]; Goldgur et al., 1997[link]; Rould et al., 1991[link]), the effects of RNA's preference for A-form helices on recognition are immediately apparent. The proteins make numerous contacts in the shallow and exposed minor grooves of the RNA helices. This contrasts with the extensive use of the major groove in the recognition of B-form DNA helices. Beyond this generalization, the details of tRNA recognition differ in each specific case. Comparison of the protein-bound tRNA to the structure of free tRNA reveals that the proteins tend to distort the RNA conformation and partially unwind the helices near the anti-codon loop. In one case, namely the structure of glutamyl-tRNA synthetase (Rould et al., 1991[link]), the final base pair near the acceptor stem of the tRNA is broken, and the CCA acceptor makes a dramatic hairpin turn into the enzyme active site.

References

First citation Cusack, S., Yaremchuk, A. & Tukalo, M. (1996a). The crystal structure of the ternary complex of T. thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site. EMBO J. 15, 2834–2842.Google Scholar
 First citation Cusack, S., Yaremchuk, A. & Tukalo, M. (1996b). The crystal structures of T. thermophilus lysyl-tRNA synthetase complexed with E. coli tRNA(Lys) and a T. thermophilus tRNA(Lys) transcript: anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue. EMBO J. 15, 6321–6334.Google Scholar
 First citation Goldgur, Y., Mosyak, L., Reshetnikova, L., Ankilova, V., Lavrik, O., Khodyreva, S. & Safro, M. (1997). The crystal structure of phenylalanyl-tRNA synthetase from Thermus Thermophilus complexed with cognate tRNAPhe. Structure, 5, 59–68.Google Scholar
 First citation Rould, M. A., Perona, J. J. & Steitz, T. A. (1991). Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature (London), 352, 213–218.Google Scholar








































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