Naslov
STRUCTURE AND FUNCTION OF UNUSUAL ARCHAEAL SERYL-tRNA SYNTHETASE

Autori
Bilokapić, Silvija ; Maier, Timm, Weygand-Durasevic, Ivana ; Ban, Nenad

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, ostalo

Izvornik
XX Congress of the International Union of crystallography / - Firenza : München, 2005

Skup
XX Congress of the International Union of crystallography

Mjesto i datum
Firenca, Italija, 23.08.2005. - 31.08.2005

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
Archaeal Seryl-tRNA synthetase

Sažetak
Inspection of the known genomic sequences reveals that two dissimilar seryl-tRNA synthetases (SerRSs) occurs in different organisms: one of bacterial type, and a diverged one present only in some members of the methanogenic archaea. We have determined the crystal structure of the diverged SerRS from Methanosarcina barkeri at 2.1 angstrom resolution, which reveals a novel and unique tRNA-binding domain among synthetases. Additionaly, the structure reveals zinc ion in the active site of the catalytic domain, which has not been observed in the structure of bacterial type SerRS. In order to understand the role of zinc ion in the mechanism of amino acid discrimination by atypical SerRS we have solved the structure of the protein in complex with serine, ATP, stable analog of seryl-adenylate, 5� -O-(N-(L-seryl)sulfamoyl)adenosine. The zinc ion is directly involved in serine recognition by forming a pentacoordinate intermediate with both the amino group and the hydroxyl group of the side chain.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA