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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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PDB id:
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Structural genomics, unknown function
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Title:
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Solution structure of a bola-like protein from mus musculus
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Structure:
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Bola-like protein riken cdna 1110025l05. Chain: a. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Other_details: cell-free protein synthesis
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NMR struc:
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20 models
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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,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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T.Kasai
et al.
(2004).
Solution structure of a BolA-like protein from Mus musculus.
Protein Sci,
13,
545-548.
PubMed id:
DOI:
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Date:
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26-Jan-04
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Release date:
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10-Feb-04
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Supersedes:
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PROCHECK
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Headers
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References
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Q8BGS2
(BOLA2_MOUSE) -
BolA-like protein 2 from Mus musculus
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Seq:
Struc:
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86 a.a.
113 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Protein Sci
13:545-548
(2004)
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PubMed id:
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Solution structure of a BolA-like protein from Mus musculus.
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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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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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Selected figure(s)
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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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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.Amicucci,
R.Balestrini,
A.Kohler,
E.Barbieri,
R.Saltarelli,
A.Faccio,
R.W.Roberson,
P.Bonfante,
and
V.Stocchi
(2011).
Hyphal and cytoskeleton polarization in Tuber melanosporum: A genomic and cellular analysis.
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Fungal Genet Biol,
48,
561-572.
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J.M.Serb,
M.C.Orr,
and
M.H.West Greenlee
(2010).
Using evolutionary conserved modules in gene networks as a strategy to leverage high throughput gene expression queries.
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PLoS One,
5,
0.
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P.J.Myler,
R.Stacy,
L.Stewart,
B.L.Staker,
W.C.Van Voorhis,
G.Varani,
and
G.W.Buchko
(2009).
The Seattle Structural Genomics Center for Infectious Disease (SSGCID).
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Infect Disord Drug Targets,
9,
493-506.
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B.Song,
J.Xiong,
C.Fang,
L.Qiu,
R.Lin,
Y.Liang,
and
W.Lin
(2008).
Allelopathic enhancement and differential gene expression in rice under low nitrogen treatment.
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J Chem Ecol,
34,
688-695.
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C.A.Hayden,
and
G.Bosco
(2008).
Comparative genomic analysis of novel conserved peptide upstream open reading frames in Drosophila melanogaster and other dipteran species.
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BMC Genomics,
9,
61.
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Y.B.Zhou,
J.B.Cao,
B.B.Wan,
X.R.Wang,
G.H.Ding,
H.Zhu,
H.M.Yang,
K.S.Wang,
X.Zhang,
and
Z.G.Han
(2008).
hBolA, novel non-classical secreted proteins, belonging to different BolA family with functional divergence.
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Mol Cell Biochem,
317,
61-68.
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B.Koch,
and
O.Nybroe
(2006).
Initial characterization of a bolA homologue from Pseudomonas fluorescens indicates different roles for BolA-like proteins in P. fluorescens and Escherichia coli.
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FEMS Microbiol Lett,
262,
48-56.
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K.H.Chin,
F.Y.Lin,
Y.C.Hu,
K.H.Sze,
P.C.Lyu,
and
S.H.Chou
(2005).
NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas campestris pv. campestris.
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J Biomol NMR,
31,
167-172.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
