1nee
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(New page: 200px<br /><applet load="1nee" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nee" /> '''Structure of archaeal translation factor aIF...)
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Revision as of 20:04, 20 November 2007
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Structure of archaeal translation factor aIF2beta from Methanobacterium thermoautrophicum
Overview
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.
About this Structure
1NEE is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: implications for translation initiation., Gutierrez P, Osborne MJ, Siddiqui N, Trempe JF, Arrowsmith C, Gehring K, Protein Sci. 2004 Mar;13(3):659-67. PMID:14978306
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