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PDBsum entry 1eif
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Initiation factor
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PDB id
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1eif
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References listed in PDB file
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Key reference
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Title
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Crystal structures of eukaryotic translation initiation factor 5a from methanococcus jannaschii at 1.8 a resolution.
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Authors
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K.K.Kim,
L.W.Hung,
H.Yokota,
R.Kim,
S.H.Kim.
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Ref.
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Proc Natl Acad Sci U S A, 1998,
95,
10419-10424.
[DOI no: ]
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PubMed id
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Abstract
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Eukaryotic translation initiation factor 5A (eIF-5A) is a ubiquitous protein
found in all eukaryotic cells. The protein is closely associated with cell
proliferation in the G1-S stage of the cell cycle. Recent findings show that the
eIF-5A proteins are highly expressed in tumor cells and act as a cofactor of the
Rev protein in HIV-1-infected cells. The mature eIF is the only protein known to
have the unusual amino acid hypusine, a post-translationally modified lysine.
The crystal structure of eIF-5A from Methanococcus jannaschii (MJ eIF-5A) has
been determined at 1.9 A and 1.8 A resolution in two crystal forms by using the
multiple isomorphous replacement method and the multiwavelength anomalous
diffraction method for the first crystal form and the molecular replacement
method for the second crystal form. The structure consists of two folding
domains, one of which is similar to the oligonucleotide-binding domain found in
the prokaryotic cold shock protein and the translation initiation factor IF1
despite the absence of any significant sequence similarities. The 12 highly
conserved amino acid residues found among eIF-5As include the hypusine site and
form a long protruding loop at one end of the elongated molecule.
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Figure 2.
Fig. 2. (A) Topology diagram of the MJ eIF-5A structure.
The arrows represent  -strands and
the short cylinder represents a 3[10] helix. The lysine
modification site is represented by a gray circle. (B) Ribbon
diagram of MJ eIF-5A structure in C2 crystal form. The arrows
represent -strands.
The secondary structures were assigned by the method of Kabsch
and Sander (31). Two domains are colored magenta and blue and
connected by a green linker. The side chain of Lys-40 is shown
as a ball-and-stick model. This figure was made with MOLSCRIPT
(32).
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Figure 6.
Fig. 6. Two different views of the surface charge
distribution of MJ eIF-5A as calculated by program GRASP (39).
The red and blue colors represent negatively and positively
charged surfaces, respectively. The lysine modification site
(Lys-40) is labeled.
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Secondary reference #1
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Title
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Cloning, Expression, And crystallization of a hyperthermophilic protein that is homologous to the eukaryotic translation initiation factor, Eif5a.
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Authors
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K.K.Kim,
H.Yokota,
R.Kim,
S.H.Kim.
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Ref.
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Protein Sci, 1997,
6,
2268-2270.
[DOI no: ]
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PubMed id
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