1efg
From Proteopedia
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THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION
Overview
Elongation factor G (EF-G) catalyzes the translocation step of protein, synthesis in bacteria, and like the other bacterial elongation factor, EF-Tu--whose structure is already known--it is a member of the GTPase, superfamily. We have determined the crystal structure of EF-G--GDP from, Thermus thermophilus. It is an elongated molecule whose large, N-terminal, domain resembles the G domain of EF-Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF-Tu, and other G proteins. The tertiary structures of the second domains of, EF-G and EF-Tu are nearly identical, but the relative placement of the, first two domains in EF-G--GDP resembles that seen in EF-Tu--GTP, not, EF-Tu--GDP. The remaining three domains of EF-G look like RNA binding, domains, and have no counterparts in EF-Tu.
About this Structure
1EFG is a Single protein structure of sequence from [1] with GDP as ligand. Full crystallographic information is available from OCA.
Reference
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 Aug 15;13(16):3661-8. PMID:8070396
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