Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

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

11/04/2010

Pubmed ID

21045311

Pubmed Central ID

PMC3001664

DOI

10.1107/S1744309110037346

Abstract

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 M

Author

Michael Kron MD Director, Professor in the Medicine department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Crystallization
Crystallography, X-Ray
Cytosol
Humans
Serine-tRNA Ligase
jenkins-FCD Prod-410 e9586552fe7f53c71f7923aa6e27aeabbd3c2473