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PDBsum entry 1ztp
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Structural genomics, unknown function
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PDB id
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1ztp
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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 structure at 2.5 a resolution of human basophilic leukemia-Expressed protein bles03.
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Authors
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E.Bitto,
C.A.Bingman,
H.Robinson,
S.T.Allard,
G.E.Wesenberg,
G.N.Phillips.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2005,
61,
812-817.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the human basophilic leukemia-expressed protein
(BLES03, p5326, Hs.433573) was determined by single-wavelength anomalous
diffraction and refined to an R factor of 18.8% (Rfree = 24.5%) at 2.5 A
resolution. BLES03 shows no detectable sequence similarity to any functionally
characterized proteins using state-of-the-art sequence-comparison tools. The
structure of BLES03 adopts a fold similar to that of eukaryotic transcription
initiation factor 4E (eIF4E), a protein involved in the recognition of the cap
structure of eukaryotic mRNA. In addition to fold similarity, the electrostatic
surface potentials of BLES03 and eIF4E show a clear conservation of basic and
acidic patches. In the crystal lattice, the acidic amino-terminal helices of
BLES03 monomers are bound within the basic cavity of symmetry-related monomers
in a manner analogous to the binding of mRNA by eIF4E. Interestingly, the gene
locus encoding BLES03 is located between genes encoding the proteins DRAP1 and
FOSL1, both of which are involved in transcription initiation. It is
hypothesized that BLES03 itself may be involved in a biochemical process that
requires recognition of nucleic acids.
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Figure 1.
Figure 1 (a) A topology diagram of the BLES03 structure (PDB
code 1ztp ). The central nine-stranded  -sheet
(red) is surrounded by several helices (cyan). The figure was
prepared using TopDraw based on a topology analysis of the
BLES03 structure by the TOPS server (Bond, 2003[Bond, C. S.
(2003). Bioinformatics, 19, 311-312.]; Westhead et al.,
1999[Westhead, D. R., Slidel, T. W., Flores, T. P. & Thornton,
J. M. (1999). Protein Sci. 8, 897-904.]). (b) A ribbon diagram
of the BLES03 structure. The structure is labeled and colored to
match the topology diagram. The figure was generated using PyMol
(DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics
System. DeLano Scientific, San Carlos, CA, USA.
http://www.pymol.org .]).
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Figure 2.
Figure 2 Structural superposition of monomer B of human BLES03
(cyan; PDB code 1ztp ) and mouse eIF4E (red; PDB code 1eh1 ).
The orientation of the structures is consistent with that
introduced in Fig. 1-. The figure was generated using PyMol
based on the structural alignment of proteins by DALI (DeLano,
2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System.
DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org .];
Holm & Sander, 1993[Holm, L. & Sander, C. (1993). J. Mol. Biol.
233, 123-138.]).
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The above figures are
reprinted
from an Open Access publication published by the IUCr:
Acta Crystallograph Sect F Struct Biol Cryst Commun
(2005,
61,
812-817)
copyright 2005.
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