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Structural genomics, unknown function
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PDB id
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1kr4
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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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Structure genomics, protein tm1056, cuta
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Structure:
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Protein tm1056, cuta. Chain: a. Engineered: yes
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Trimer (from PDB file)
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Resolution:
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1.40Å
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R-factor:
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0.218
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R-free:
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0.241
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Authors:
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A.Savchenko,R.Zhang,A.Joachimiak,A.Edwards,T.Akarina,Midwest For Structural Genomics (Mcsg)
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Key ref:
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A.Savchenko
et al.
(2004).
X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A resolution.
Proteins,
54,
162-165.
PubMed id:
DOI:
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Date:
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08-Jan-02
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Release date:
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14-Aug-02
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PROCHECK
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Headers
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References
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Q9X0E6
(CUTA_THEMA) -
Divalent-cation tolerance protein CutA
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Seq:
Struc:
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101 a.a.
110 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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response to metal ion
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1 term
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DOI no:
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Proteins
54:162-165
(2004)
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PubMed id:
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X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A resolution.
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A.Savchenko,
T.Skarina,
E.Evdokimova,
J.D.Watson,
R.Laskowski,
C.H.Arrowsmith,
A.M.Edwards,
A.Joachimiak,
R.G.Zhang.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. Multiple sequence alignment of CutA from Thermotoga
maritima (Thema) against other periplasmic divalent cation
tolerance proteins from bacteria (Aquae = Aquifex aeolicus,
Deira = Deinococcus radiodurans) and archaea (Pyrho = Pyrococcus
horikoshii, Arcfu = Archaeoglobus fulgidus, Thevo = Thermoplasma
volcanium), together with one from Mouse and a brain
acetylcholinesterase putative membrane anchor from Human.
Sequence conservation is color coded from red for invariant
residues to orange to grey to none. The secondary structure of
the T. maritima CutA is schematically shown in purple above the
alignment.
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Figure 2.
Figure 2. Ribbon representations of the tmCutA monomer (a),
trimer (b) and superimposed structures of tmCutA and GlnK'
complex with ATP (c). a: The  -helixes
and  -strains
are colored in red and blue, respectively. b: Each monomer in
the tmCutA trimer is differentiated by color. c: The tmCutA is
shown on green, GnlK is shown in blue and ATP molecules are
colored in red.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
54,
162-165)
copyright 2004.
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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.Sato,
S.Yokotani,
T.Tadokoro,
S.Tanaka,
C.Angkawidjaja,
Y.Koga,
K.Takano,
and
S.Kanaya
(2011).
Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella sp. SIB1.
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J Synchrotron Radiat, 18,
6.
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PDB code:
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D.Liang,
S.Carvalho,
S.Bon,
and
J.Massoulié
(2009).
Unusual transfer of CutA into the secretory pathway, evidenced by fusion proteins with acetylcholinesterase.
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FEBS J, 276,
4473-4482.
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J.Yang,
H.Yang,
L.Yan,
L.Yang,
and
L.Yu
(2009).
Characterization of the human CUTA isoform2 present in the stably transfected HeLa cells.
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Mol Biol Rep, 36,
63-69.
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B.Bagautdinov,
Y.Matsuura,
S.Bagautdinova,
N.Kunishima,
and
K.Yutani
(2008).
Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 64,
351-357.
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PDB code:
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M.H.Godsey,
G.Minasov,
L.Shuvalova,
J.S.Brunzelle,
I.I.Vorontsov,
F.R.Collart,
and
W.F.Anderson
(2007).
The 2.2 A resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain.
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Protein Sci, 16,
1285-1293.
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PDB code:
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C.H.Lin,
K.H.Chin,
F.P.Gao,
P.C.Lyu,
H.L.Shr,
A.H.Wang,
and
S.H.Chou
(2006).
Cloning, crystallization and preliminary X-ray studies of XC2981 from Xanthomonas campestris, a putative CutA1 protein involved in copper-ion homeostasis.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
1113-1115.
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S.B.Conners,
E.F.Mongodin,
M.R.Johnson,
C.I.Montero,
K.E.Nelson,
and
R.M.Kelly
(2006).
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
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FEMS Microbiol Rev, 30,
872-905.
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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
