1b64
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SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES
OverviewOverview
BACKGROUND: 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 ... [(full description)]
About this StructureAbout this Structure
1B64 is a [Single protein] structure of sequence from [Homo sapiens]. Structure known Active Site: GEF. Full crystallographic information is available from [OCA].
ReferenceReference
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., Perez JM, Siegal G, Kriek J, Hard K, Dijk J, Canters GW, Moller W, Structure. 1999 Feb 15;7(2):217-26. PMID:10368288
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