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PMID: 8070396 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.

The EMBO journal ·Vol. 13 ·No. 16 ·1994-08-15 ·Pages 3661-8

Czworkowski J, Wang J, Steitz TA, Moore PB

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.

MeSH Terms
Amino Acid Sequence Binding Sites Crystallography, X-Ray GTP Phosphohydrolase-Linked Elongation Factors/chemistry,metabolism Guanosine Diphosphate/chemistry Models, Molecular Molecular Sequence Data Peptide Chain Elongation, Translational Peptide Elongation Factor G Peptide Elongation Factor Tu/chemistry Peptide Elongation Factors/chemistry,metabolism Thermus thermophilus/chemistry,enzymology
Chemicals
Peptide Elongation Factor G Peptide Elongation Factors Guanosine Diphosphate GTP Phosphohydrolase-Linked Elongation Factors Peptide Elongation Factor Tu
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Czworkowski J
Department of Chemistry, Yale University, New Haven, CT 06520.
Wang J
Steitz T A
Moore P B
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1994-08-15
Pages
3661-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC395276
Subset
IM
Grants
NIAID NIH HHS · AI-09167 · United States
NIGMS NIH HHS · GM22778 · United States
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