Crystallization and preliminary X-ray diffraction analysis of human cytosolic seryl-tRNA synthetase. Acta Crystallogr Sect F Struct Biol Cryst Commun 2010 Nov 01;66(Pt 11):1521-4
Date
11/04/2010Pubmed ID
21045311Pubmed Central ID
PMC3001664DOI
10.1107/S1744309110037346Abstract
Human cytosolic seryl-tRNA synthetase (hsSerRS) is responsible for the covalent attachment of serine to its cognate tRNA(Ser). Significant differences between the amino-acid sequences of eukaryotic, prokaryotic and archaebacterial SerRSs indicate that the domain composition of hsSerRS differs from that of its eubacterial and archaebacterial analogues. As a consequence of an N-terminal insertion and a C-terminal extra-sequence, the binding mode of tRNA(Ser) to hsSerRS is expected to differ from that in prokaryotes. Recombinant hsSerRS protein was purified to homogeneity and crystallized. Diffraction data were collected to 3.13 Å resolution. The structure of hsSerRS has been solved by the molecular-replacement method.
Author List
Artero JB, Teixeira SC, Mitchell EP, Kron MA, Forsyth VT, Haertlein MAuthor
Michael Kron MD Director, Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
CrystallizationCrystallography, X-Ray
Cytosol
Humans
Serine-tRNA Ligase
