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

Amit Priyadarshi, Ki Hyun Nam, Eunice Eunkyeong Kim, Kwang Yeon Hwang

Research output: Contribution to journalArticle

Abstract

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 Å 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 Å, α = β = γ = 90°. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding V M of 2.4 Å 3 Da -1 and a solvent content of 50%.

Original languageEnglish
Pages (from-to)1166-1168
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number12
DOIs
Publication statusPublished - 2008 Nov 28

Fingerprint

staphylococcus
GTP Phosphohydrolases
Transfer RNA
Crystallization
Staphylococcus aureus
enzymes
X-Rays
crystallization
X rays
ammonium sulfates
guanines
nucleotides
Escherichia
bacteria
crystals
synchrotron radiation
Crystals
Synchrotrons
x rays
Guanine Nucleotides

Keywords

  • GDP
  • GTP
  • GTPases
  • Probable tRNA modification
  • Staphylococcus aureus
  • TrmE

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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title = "Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus",
abstract = "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 {\AA} 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 {\AA}, α = β = γ = 90°. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding V M of 2.4 {\AA} 3 Da -1 and a solvent content of 50{\%}.",
keywords = "GDP, GTP, GTPases, Probable tRNA modification, Staphylococcus aureus, TrmE",
author = "Amit Priyadarshi and Nam, {Ki Hyun} and Kim, {Eunice Eunkyeong} and Hwang, {Kwang Yeon}",
year = "2008",
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T1 - Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus

AU - Priyadarshi, Amit

AU - Nam, Ki Hyun

AU - Kim, Eunice Eunkyeong

AU - Hwang, Kwang Yeon

PY - 2008/11/28

Y1 - 2008/11/28

N2 - 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 Å 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 Å, α = β = γ = 90°. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding V M of 2.4 Å 3 Da -1 and a solvent content of 50%.

AB - 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 Å 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 Å, α = β = γ = 90°. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding V M of 2.4 Å 3 Da -1 and a solvent content of 50%.

KW - GDP

KW - GTP

KW - GTPases

KW - Probable tRNA modification

KW - Staphylococcus aureus

KW - TrmE

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