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PDBsum entry 1v9j
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Structural genomics, unknown function
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PDB id
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1v9j
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of a bola-Like protein from mus musculus.
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Authors
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T.Kasai,
M.Inoue,
S.Koshiba,
T.Yabuki,
M.Aoki,
E.Nunokawa,
E.Seki,
T.Matsuda,
N.Matsuda,
Y.Tomo,
M.Shirouzu,
T.Terada,
N.Obayashi,
H.Hamana,
N.Shinya,
A.Tatsuguchi,
S.Yasuda,
M.Yoshida,
H.Hirota,
Y.Matsuo,
K.Tani,
H.Suzuki,
T.Arakawa,
P.Carninci,
J.Kawai,
Y.Hayashizaki,
T.Kigawa,
S.Yokoyama.
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Ref.
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Protein Sci, 2004,
13,
545-548.
[DOI no: ]
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PubMed id
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Abstract
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The BolA-like proteins are widely conserved from prokaryotes to eukaryotes. The
BolA-like proteins seem to be involved in cell proliferation or cell-cycle
regulation, but the molecular function is still unknown. Here we determined the
structure of a mouse BolA-like protein. The overall topology is
alphabetabetaalphaalphabetaalpha, in which beta(1) and beta(2) are antiparallel,
and beta(3) is parallel to beta(2). This fold is similar to the class II KH
fold, except for the absence of the GXXG loop, which is well conserved in the KH
fold. The conserved residues in the BolA-like proteins are assembled on the one
side of the protein.
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Figure 2.
Figure 2. (A) The conserved residues on the surface of the
mouse BolA2. The identical and the similar residues defined in
Figure 1A Go- are colored
dark blue and light blue, respectively. The right panel is
viewed from the opposite side of the left panel. (B) The surface
electrostatic potential of BolA2. (C) Ribbon diagram in the same
orientation as A and B. The HTH motif is indicated by the blue
circle.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2004,
13,
545-548)
copyright 2004.
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