Elongation factor G (EF-G) catalyzes the translocation step of translation. It consists of five structural domains, this entry represents the second domain [1]. This domain adopts a beta barrel structure. This family also includes domains found in other translation factors such as translation initiation factor IF-2, peptide chain release factor, etc. Paper describing PDB structure 1dar. [1]. 8736554. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A;. Structure. 1996;4:555-565. Paper describing PDB structure 1efg. [2]. 8070396. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. Czworkowski J, Wang J, Steitz TA, Moore PB;. EMBO J. 1994;13:3661-3668. Paper describing PDB structure 1eft. [3]. 8069622. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Kjeldgaard M, Nissen P, Thirup S, Nyborg J;. Structure. 1993;1:35-50. Paper describing PDB structure 1fnm. [4]. 11054294. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A;. J Mol Biol. 2000;303:593-603. Paper describing PDB structure 1g7r. [5]. 11114334. X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. Roll-Mecak A, Cao C, Dever TE, Burley SK;. Cell. 2000;103:781-792. (from Pfam)
- Date:
- 2024-10-16