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Krystalstruktur af det katalytiske domæne af eIF2Be

Activity: Talk or presentation typesLecture and oral contribution

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Thomas Boesen - Lecturer

  • Department of Molecular Biology
The crystal structure of the C-terminal catalytic domain of the eukaryotic initiation factor 2B epsilon subunit, residues 544-704, from Saccharomyces cerevisiae has been determined to 2.3 Å resolution by the multiple wavelength anomalous dispersion technique using selenomethionine substituted protein. The structure consists of eight alpha-helices arranged in a manner similar to HEAT repeats. The N-terminal two helices contain the catalytic part of the domain, whereas the C-terminal six helices harbor the two Aromatic Acidic (AA) box motifs involved in binding to the N-terminal part of the initiation factor 2b subunit. Aliphatic residues in the AA box motifs are involved in specific contacts in the hydrophobic core of the C-terminal bundle important for maintaining the overall structure, whereas acidic residues in the motifs form a clustered, surface exposed acidic patch which might interact with the lysine boxes of initiation factor 2b. Interestingly, Tryptophan 699 was found to be solvent exposed and involved in crystal packing. This residue could possibly be important for the specific interaction with initiation factor 2b. Furthermore, the structure shows the location of residues important for catalytic function and disease.
Emneord: protein synthesis, initiation
8 Sep 2004

Event (Conference)

TitleTranslational Control Meeting 2004
CityCold Spring Harbor Laboratory, NY
CountryUnited States


  • protein synthesis, initiation

ID: 425817