Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2

Sylvie Meunier; Roberto Spurio; Michael Czisch; Rainer Wechselberger; Marc Guenneugues; Claudio O. Gualerzi; Rolf Boelens

Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2

Sylvie Meunier, Roberto Spurio, Michael Czisch, Rainer Wechselberger, Marc Guenneugues, Claudio O. Gualerzi, Rolf Boelens

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The three-dimensional structure of the fMet-tRNA(fMet)-binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel β-strands, connected via loops, and forms a closed β-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu·aminoacyl-tRNA·GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.

Original language	English
Pages (from-to)	1918-1926
Number of pages	9
Journal	EMBO Journal
Volume	19
Issue number	8
Publication status	Published - 17 Apr 2000

Keywords

Bacterial translation
NMR
Protein
Protein biosynthesis
Ribosome
guanosine diphosphate
initiation factor 2
transfer RNA
article
Geobacillus stearothermophilus
nonhuman
nuclear magnetic resonance
priority journal
protein quaternary structure
protein RNA binding
sequence homology

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title = "Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2",

abstract = "The three-dimensional structure of the fMet-tRNA(fMet)-binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel β-strands, connected via loops, and forms a closed β-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu·aminoacyl-tRNA·GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.",

keywords = "Bacterial translation, NMR, Protein, Protein biosynthesis, Ribosome, guanosine diphosphate, initiation factor 2, transfer RNA, article, Geobacillus stearothermophilus, nonhuman, nuclear magnetic resonance, priority journal, protein quaternary structure, protein RNA binding, sequence homology",

author = "Sylvie Meunier and Roberto Spurio and Michael Czisch and Rainer Wechselberger and Marc Guenneugues and Gualerzi, {Claudio O.} and Rolf Boelens",

year = "2000",

month = apr,

day = "17",

language = "English",

volume = "19",

pages = "1918--1926",

journal = "EMBO Journal",

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TY - JOUR

T1 - Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2

AU - Meunier, Sylvie

AU - Spurio, Roberto

AU - Czisch, Michael

AU - Wechselberger, Rainer

AU - Guenneugues, Marc

AU - Gualerzi, Claudio O.

AU - Boelens, Rolf

PY - 2000/4/17

Y1 - 2000/4/17

N2 - The three-dimensional structure of the fMet-tRNA(fMet)-binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel β-strands, connected via loops, and forms a closed β-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu·aminoacyl-tRNA·GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.

AB - The three-dimensional structure of the fMet-tRNA(fMet)-binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel β-strands, connected via loops, and forms a closed β-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu·aminoacyl-tRNA·GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.

KW - Bacterial translation

KW - NMR

KW - Protein

KW - Protein biosynthesis

KW - Ribosome

KW - guanosine diphosphate

KW - initiation factor 2

KW - transfer RNA

KW - article

KW - Geobacillus stearothermophilus

KW - nonhuman

KW - nuclear magnetic resonance

KW - priority journal

KW - protein quaternary structure

KW - protein RNA binding

KW - sequence homology

M3 - Article

SN - 0261-4189

VL - 19

SP - 1918

EP - 1926

JO - EMBO Journal

JF - EMBO Journal

IS - 8

ER -

Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2

Abstract

Keywords

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