ZIB

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

The class II aminoacyl-tRNA synthetases and their active site: Evolutionary conservation of an ATP binding site (1995)

Eriani, Gilbert ; Cavarelli, Jean ; Martin, Franck ; [et al.]

Springer

Journal of molecular evolution 40 (1995), S. 499-508

add to mindlist on the mindlist

Details

ISSN: 1432-1432

Keywords: Two classes of aminoacyl-tRNA synthetases ; Sequence comparisons ; Homology ; X-ray structure ; Structure-function relationships ; Origin of aminoacyl-tRNA synthetases ; Two ancestral molecules ; Genetic code

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Previous sequence analyses have suggested the existence of two distinct classes of aminoacyl-tRNA synthetase. The partition was established on the basis of exclusive sets of sequence motifs (Eriani et al. [1990] Nature 347:203–306). X-ray studies have now well defined the structural basis of the two classes: the class I enzymes share with dehydrogenases and kinases the classic nucleotide binding fold called the Rossmann fold, whereas the class II enzymes possess a different fold, not found elsewhere, built around a six-stranded antiparallel β-sheet. The two classes of synthetases catalyze the same global reaction that is the attachment of an amino acid to the tRNA, but differ as to where on the terminal adenosine of the tRNA the amino acid is placed: class I enzymes act on the 2′ hydroxyl whereas the class II enzymes prefer the 3′ hydroxyl group. The three-dimensional structure of aspartyl-tRNA synthetase from yeast, a typical class II enzyme, is described here, in relation to its function. The crucial role of the sequence motifs in substrate binding and enzyme structure is high-lighted. Overall these results underline the existence of an intimate evolutionary link between the aminoacyl-tRNA synthetases, despite their actual structural diversity.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00166618

Permalink

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs (1990)

Eriani, Gilbert ; Delarue, Marc ; Poch, Olivier ; [et al.]

[s.l.] : Nature Publishing Group

Nature 347 (1990), S. 203-206

add to mindlist on the mindlist

Details

ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] To clone the ProRS gene, a pool of partially digested E. coli DNA fragments was used to transform and complement the strain UQ27 (proS27, argG, lac, thi), a temperature-sensitive mutant defective in ProRS activity5. From complementing trans- formants we isolated several types of plasmids, whose ...