1NEE
Structure of archaeal translation factor aIF2beta from Methanobacterium thermoautrophicum
Summary for 1NEE
| Entry DOI | 10.2210/pdb1nee/pdb |
| NMR Information | BMRB: 5312 |
| Descriptor | Probable translation initiation factor 2 beta subunit, ZINC ION (2 entities in total) |
| Functional Keywords | two domain protein, mixed alpha-beta structure, zinc finger, translation |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 15958.67 |
| Authors | Gutierrez, P.,Trempe, J.F.,Siddiqui, N.,Arrowsmith, C.,Gehring, K. (deposition date: 2002-12-11, release date: 2004-03-09, Last modification date: 2024-05-22) |
| Primary citation | Gutierrez, P.,Osborne, M.J.,Siddiqui, N.,Trempe, J.F.,Arrowsmith, C.,Gehring, K. Structure of the archaeal translation initiation factor aIF2beta from Methanobacterium thermoautotrophicum: Implications for translation initiation. Protein Sci., 13:659-667, 2004 Cited by PubMed Abstract: 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. PubMed: 14978306DOI: 10.1110/ps.03506604 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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