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Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: implications for translation initiation

Gutiérrez, P.; Osborne, M.J.; Siddiqui, N.; Trempe, J-François.; Arrowsmith, C.; Gehring, K.

Protein Science: a Publication of the Protein Society 13(3): 659-667

2004


ISSN/ISBN: 0961-8368
PMID: 14978306
DOI: 10.1110/ps.03506604
Accession: 050399588

aIF2 beta is the archaeal homolog of eIF2 beta, a member of the eIF2 heterotrimeric complex, implicated in the delivery of Met-tRNA(i)(Met) to the 40S ribosomal subunit. We have determined the solution structure of the intact beta-subunit of aIF2 from Methanobacterium thermoautotrophicum. aIF2 beta is composed of an unfolded N terminus, a mixed alpha/beta core domain and a C-terminal zinc finger. NMR data shows the two folded domains display restricted mobility with respect to each other. Analysis of the aIF2 gamma structure docked to tRNA allowed the identification of a putative binding site for the beta-subunit in the ternary translation complex. Based on structural similarity and biochemical data, a role for the different secondary structure elements is suggested.

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