1k8b

NMR Structure Analysis of the N-terminal Domain of Archaeal Translation Initiation Factor 2 Subunit beta

spinqualitylabelsall models 1k8b Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k8b is a 1 chain structure with sequence from Methanocaldococcus jannaschii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IF2B_METJA eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins.,Cho S, Hoffman DW Biochemistry. 2002 May 7;41(18):5730-42. PMID:11980477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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