1D1N

SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2

Summary for 1D1N

• Entry DOI: 10.2210/pdb1d1n/pdb
• NMR Information: BMRB: 4697
• Descriptor: INITIATION FACTOR 2 (1 entity in total)
• Functional Keywords: beta-barrel, gene regulation
• Biological source: Geobacillus stearothermophilus
• Cellular location: Cytoplasm: P04766
• Total number of polymer chains: 1
• Total formula weight: 11210.74

Authors

Meunier, S.,Spurio, S.,Czisch, M.,Wechselberger, R.,Gueunneugues, M. (deposition date: 1999-09-20, release date: 2000-09-20, Last modification date: 2024-05-22)

Primary citation

Meunier, S.,Spurio, R.,Czisch, M.,Wechselberger, R.,Guenneugues, M.,Gualerzi, C.O.,Boelens, R.
Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2.
EMBO J., 19:1918-1926, 2000

PubMed 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 beta-strands, connected via loops, and forms a closed beta-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 small middle dotaminoacyl-tRNA small middle dot GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.

PubMed: 10775275
DOI: 10.1093/emboj/19.8.1918

Experimental method

SOLUTION NMR