Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

P Nissen; L Reshetnikova; G Siboska; G Polekhina; S Thirup; M Kjeldgaard; B F Clark; J Nyborg

Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

P Nissen, L Reshetnikova, G Siboska, G Polekhina, S Thirup, M Kjeldgaard, B F Clark, J Nyborg

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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Abstract

Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-Tu binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-Tu:GTP:aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-Tu:GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-Tu:GDPNP and yeast Phe-tRNA(Phe) after its purification by HPLC.

Original language	English
Journal	FEBS Letters
Volume	356
Issue	2-3
Pages (from-to)	165-8
Number of pages	3
ISSN	0014-5793
Publication status	Published - 1994

Keywords

Chromatography, Gel
Chromatography, High Pressure Liquid
Crystallization
Crystallography, X-Ray
Electrophoresis, Polyacrylamide Gel
Guanosine Triphosphate
Guanylyl Imidodiphosphate
Peptide Elongation Factor Tu
RNA, Transfer, Phe
Saccharomyces cerevisiae
Thermus

Cite this

@article{43529f10f9c311dd8f9a000ea68e967b,

title = "Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)",

abstract = "Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-Tu binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-Tu:GTP:aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-Tu:GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-Tu:GDPNP and yeast Phe-tRNA(Phe) after its purification by HPLC.",

keywords = "Chromatography, Gel, Chromatography, High Pressure Liquid, Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Peptide Elongation Factor Tu, RNA, Transfer, Phe, Saccharomyces cerevisiae, Thermus",

author = "P Nissen and L Reshetnikova and G Siboska and G Polekhina and S Thirup and M Kjeldgaard and Clark, {B F} and J Nyborg",

year = "1994",

language = "English",

volume = "356",

pages = "165--8",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley & Sons Inc.",

number = "2-3",

}

TY - JOUR

T1 - Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

AU - Nissen, P

AU - Reshetnikova, L

AU - Siboska, G

AU - Polekhina, G

AU - Thirup, S

AU - Kjeldgaard, M

AU - Clark, B F

AU - Nyborg, J

PY - 1994

Y1 - 1994

N2 - Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-Tu binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-Tu:GTP:aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-Tu:GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-Tu:GDPNP and yeast Phe-tRNA(Phe) after its purification by HPLC.

AB - Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-Tu binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-Tu:GTP:aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-Tu:GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-Tu:GDPNP and yeast Phe-tRNA(Phe) after its purification by HPLC.

KW - Chromatography, Gel

KW - Chromatography, High Pressure Liquid

KW - Crystallization

KW - Crystallography, X-Ray

KW - Electrophoresis, Polyacrylamide Gel

KW - Guanosine Triphosphate

KW - Guanylyl Imidodiphosphate

KW - Peptide Elongation Factor Tu

KW - RNA, Transfer, Phe

KW - Saccharomyces cerevisiae

KW - Thermus

M3 - Journal article

C2 - 7805830

SN - 0014-5793

VL - 356

SP - 165

EP - 168

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

Abstract

Keywords

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