1K81

NMR Structure of the Zinc-Ribbon Domain within Translation Initiation Factor 2 Subunit beta

1K81 の概要

• エントリーDOI: 10.2210/pdb1k81/pdb
• 関連するPDBエントリー: 1K8B
• NMR情報: BMRB: 5294
• 分子名称: PROBABLE TRANSLATION INITIATION FACTOR 2 BETA SUBUNIT, ZINC ION (2 entities in total)
• 機能のキーワード: translation initiation factor, zinc ribbon, translation
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4127.51

構造登録者

Cho, S.,Hoffman, D.W. (登録日: 2001-10-22, 公開日: 2002-04-24, 最終更新日: 2024-05-22)

主引用文献

Cho, S.,Hoffman, D.W.
Structure of the beta Subunit of Translation Initiation Factor 2 from the Archaeon Methanococcus jannaschii: A Representative of the eIF2beta/eIF5 Family of Proteins
Biochemistry, 41:5730-5742, 2002

PubMed Abstract: The beta subunit of archaeal translation initiation factor 2 (aIF2beta) is a representative of a family of proteins whose members include the beta subunit of eukaryotic translation initiation factor 2 (eIF2beta) and the N-terminal domain within translation initiation factor 5 (eIF5); no members of this family of proteins have been structurally characterized up to this time. In the work presented here, aIF2beta from Methanococcus jannaschii was expressed in Escherichia coli, purified, and analyzed using multidimensional NMR methods. The aIF2beta was found to contain two independent structural domains. The N-terminal domain contains a four-stranded antiparallel beta sheet and two alpha helices, and is structurally similar to the DNA-binding domain of a yeast heat shock transcription factor and a domain within ribosomal protein S4. This structural similarity was an unanticipated result, since no significant homology was detected at the level of primary sequence. The C-terminal domain of aIF2beta contains a zinc-binding motif of three antiparallel beta strands, with four conserved cysteines arranged as two CXXC units separated by 17 residues. Conserved residues on the surface of each domain that are likely candidates for direct interaction with other components of the translational apparatus were identified. The significant primary sequence homology between archaeal aIF2beta and the eukaryotic eIF2beta and eIF5, when combined with the structural results in the work presented here, permitted structural features to be predicted for these latter two eukaryotic proteins.

PubMed: 11980477
DOI: 10.1021/bi011984n

実験手法

SOLUTION NMR