2EFG

TRANSLATIONAL ELONGATION FACTOR G COMPLEXED WITH GDP

Summary for 2EFG

• Entry DOI: 10.2210/pdb2efg/pdb
• Descriptor: PROTEIN (ELONGATION FACTOR G), PROTEIN (ELONGATION FACTOR G DOMAIN 3), GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: elongation factor, translocase, ribosome, elongation, translation, protein synt factor, gtpase, gtp binding, guanosine nucleotide binding, protein binding
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: P13551
• Total number of polymer chains: 2
• Total formula weight: 84913.52

Authors

Czworkowski, J.,Wang, J.,Steitz, T.A.,Moore, P.B. (deposition date: 1998-09-23, release date: 1999-09-30, Last modification date: 2023-08-23)

Primary citation

Czworkowski, J.,Wang, J.,Steitz, T.A.,Moore, P.B.
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
EMBO J., 13:3661-3668, 1994

PubMed Abstract: 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.

PubMed: 8070396

Experimental method

X-RAY DIFFRACTION (2.6 Å)