Structural highlights
3cw2 is a 12 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Gene: | eif2g, SSO0412 (ATCC 35091), eif2a, SSO1050 (ATCC 35091), eif2b, SSO2381 (ATCC 35091) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[IF2G_SULSO] eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (By similarity). [IF2B_SULSO] eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (By similarity). [IF2A_SULSO] 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
In Eukarya and Archaea, translation initiation factor 2 (eIF2/aIF2), which contains three subunits (alpha, beta, and gamma), is pivotal for binding of charged initiator tRNA to the small ribosomal subunit. The crystal structure of the full-sized heterotrimeric aIF2 from Sulfolobus solfataricus in the nucleotide-free form has been determined at 2.8-A resolution. Superposition of four molecules in the asymmetric unit of the crystal and the comparison of the obtained structures with the known structures of the aIF2alphagamma and aIF2betagamma heterodimers revealed high conformational flexibility in the alpha- and beta-subunits. In fact, the full-sized aIF2 consists of a rigid central part, formed by the gamma-subunit, domain 3 of the alpha-subunit, and the N-terminal alpha-helix of the beta-subunit, and two mobile "wings," formed by domains 1 and 2 of the alpha-subunit, the central part, and the zinc-binding domain of the beta-subunit. High structural flexibility of the wings is probably required for interaction of aIF2 with the small ribosomal subunit. Comparative analysis of all known structures of the gamma-subunit alone and within the heterodimers and heterotrimers in nucleotide-bound and nucleotide-free states shows that the conformations of switch 1 and switch 2 do not correlate with the assembly or nucleotide states of the protein.
Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits.,Stolboushkina E, Nikonov S, Nikulin A, Blasi U, Manstein DJ, Fedorov R, Garber M, Nikonov O J Mol Biol. 2008 Oct 10;382(3):680-91. Epub 2008 Jul 22. PMID:18675278[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stolboushkina E, Nikonov S, Nikulin A, Blasi U, Manstein DJ, Fedorov R, Garber M, Nikonov O. Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits. J Mol Biol. 2008 Oct 10;382(3):680-91. Epub 2008 Jul 22. PMID:18675278 doi:http://dx.doi.org/S0022-2836(08)00881-4
