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PDBsum entry 1b64
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Guanine nucleotide exchange factor
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PDB id
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1b64
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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J.M.Pérez,
G.Siegal,
J.Kriek,
K.Hård,
J.Dijk,
G.W.Canters,
W.Möller.
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Ref.
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Structure, 1999,
7,
217-226.
[DOI no: ]
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PubMed id
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Abstract
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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 explore whether the prokaryotic exchange mechanism could shed any
light on the mechanism of eukaryotic translation elongation. RESULTS: Here, we
report the structure of the guanine-nucleotide exchange factor (GEF) domain of
human EF-1beta (hEF-1beta, residues 135-224); hEF-1beta[135-224], determined by
nuclear magnetic resonance spectroscopy. Sequence conservation analysis of the
GEF domains of EF-1 subunits beta and delta from widely divergent organisms
indicates that the most highly conserved residues are in two loop regions.
Intriguingly, hEF-1beta[135-224] shares structural homology with the GEF domain
of EF-Ts despite their different primary sequences. CONCLUSIONS: On the basis of
both the structural homology between EF-Ts and hEF-1beta[135-224] and the
sequence conservation analysis, we propose that the mechanism of
guanine-nucleotide exchange in protein synthesis has been conserved in
prokaryotes and eukaryotes. In particular, Tyr181 of hEF-1beta[135-224] appears
to be analogous to Phe81 of Escherichia coli EF-Ts.
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Figure 6.
Figure 6. Comparison of the tertiary structure of EF-1β and
the GEF domain of EF-Ts. (a) Side-by-side ribbon diagrams of the
GEF domain of E. coli EF-Ts (residues 57–139) and
hEF-1β[135–224]. The structure on the left is the GEF-domain
of EF-Ts (α helices in red and yellow, β sheet in cyan) from
the complex with EF-Tu [20] . The sPhe81 sidechain is shown in
dark blue. The mean structure of hEF-1β[135–224] (α helices
in green and yellow, β sheet in dark blue) is shown on the
right, with the loop between β2 and β3 in magenta and
the sidechain of Tyr181 in yellow. (b) Superposition of the GEF
domain of EF-Ts and hEF-1β[135–224]. The color scheme is
identical to that in (a). Nineteen Cα atoms from each structure
were chosen for a least-squares superposition. This figure was
prepared using the program MOLMOL [54] .
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The above figure is
reprinted
by permission from Cell Press:
Structure
(1999,
7,
217-226)
copyright 1999.
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Secondary reference #1
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Title
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1h, 15n and 13c chemical shift assignment of the guanine nucleotide exchange domain of human elongation factor-One beta.
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Authors
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J.M.Pérez,
J.Kriek,
J.Dijk,
W.Möller,
G.Siegal,
K.Hård,
A.P.Kalverda,
G.W.Canters.
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Ref.
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J Biomol Nmr, 1998,
12,
467-468.
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PubMed id
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