Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus

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초록

Probable tRNA-modification GTPase (TrmE) is a guanine nucleotide-binding protein that is conserved between bacteria and humans. GTPase hydrolyzes GTP and plays a pivotal role in signalling pathways. In this study, TrmE from Staphylococcus aureus was overexpressed in Escherichia coli. The enzyme was found to crystallize at 295 K when ammonium sulfate was used as a precipitant. X-ray diffraction data were collected to 2.9 angstrom resolution from the crystallized enzyme using synchrotron radiation. The crystal was found to belong to the cubic space group I23, with unit-cell parameters a = b = c = 229.47 angstrom, alpha = beta = gamma = 90 degrees. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding V-M of 2.4 angstrom 3 Da(-1) and a solvent content of 50%.

키워드

GDPGTPGTPasesProbable tRNA modificationStaphylococcus aureusTrmECOLI MNME PROTEIN
제목
Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus
저자
Priyadarshi, AmitNam, Ki HyunKim, Eunice EunKyeongHwang, Kwang Yeon
DOI
10.1107/S1744309108036579
발행일
2008-12
유형
Article
저널명
Acta Crystallographica Section F: Structural Biology Communications
64
페이지
1166 ~ 1168