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Crystallization and preliminary X-ray diffraction analysis of human cytosolic seryl-tRNA synthetase.

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.

SUBMITTER: Artero JB

PROVIDER: S-EPMC3001664 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of human cytosolic seryl-tRNA synthetase.

Artero Jean Baptiste JB Teixeira Susana C M SC Mitchell Edward P EP Kron Michael A MA Forsyth V Trevor VT Haertlein Michael M

Acta crystallographica. Section F, Structural biology and crystallization communications 20101029 Pt 11

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 t ...[more]

PMID: 21045311

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