1B64

SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES

Summary for 1B64

• Entry DOI: 10.2210/pdb1b64/pdb
• Descriptor: ELONGATION FACTOR 1-BETA (1 entity in total)
• Functional Keywords: guanine nucleotide exchange factor, g-protein, translation elongation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 10148.63

Authors

Perez, J.M.J.,Siegal, G.,Kriek, J.,Hard, K.,Dijk, J.,Canters, G.W.,Moller, W. (deposition date: 1999-01-20, release date: 1999-05-18, Last modification date: 2024-05-22)

Primary citation

Perez, J.M.,Siegal, G.,Kriek, J.,Hard, K.,Dijk, J.,Canters, G.W.,Moller, W.
The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli.
Structure Fold.Des., 7:217-226, 1999

PubMed Abstract: In eukaryotic protein synthesis, the multi-subunit elongation factor 1 (EF-1) plays an important role in ensuring the fidelity and regulating the rate of translation. EF-1alpha, which transports the aminoacyl tRNA to the ribosome, is a member of the G-protein superfamily. EF-1beta regulates the activity of EF-1alpha by catalyzing the exchange of GDP for GTP and thereby regenerating the active form of EF-1alpha. The structure of the bacterial analog of EF-1alpha, EF-Tu has been solved in complex with its GDP exchange factor, EF-Ts. These structures indicate a mechanism for GDP-GTP exchange in prokaryotes. Although there is good sequence conservation between EF-1alpha and EF-Tu, there is essentially no sequence similarity between EF-1beta and EF-Ts. We wished to explore whether the prokaryotic exchange mechanism could shed any light on the mechanism of eukaryotic translation elongation.

PubMed: 10368288
DOI: 10.1016/S0969-2126(99)80027-6

Experimental method

SOLUTION NMR