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PDBsum entry 1st7
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Transport protein
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PDB id
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1st7
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Contents |
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* Residue conservation analysis
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PDB id:
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Transport protein
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Title:
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Solution structure of acyl coenzyme a binding protein from yeast
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Structure:
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Acyl-coa-binding protein. Chain: a. Synonym: acbp. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: acb1, acb, ygr037c. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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K.Teilum,T.Thormann,N.R.Caterer,H.I.Poulsen,P.H.Jensen,J.Knudsen, B.B.Kragelund,F.M.Poulsen
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Key ref:
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K.Teilum
et al.
(2005).
Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles.
Proteins,
59,
80-90.
PubMed id:
DOI:
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Date:
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25-Mar-04
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Release date:
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01-Mar-05
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PROCHECK
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Headers
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References
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P31787
(ACBP_YEAST) -
Acyl-CoA-binding protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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87 a.a.
86 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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Proteins
59:80-90
(2005)
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PubMed id:
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Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles.
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K.Teilum,
T.Thormann,
N.R.Caterer,
H.I.Poulsen,
P.H.Jensen,
J.Knudsen,
B.B.Kragelund,
F.M.Poulsen.
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ABSTRACT
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Comparison of the folding processes for homologue proteins can provide valuable
information about details in the interactions leading to the formation of the
folding transition state. Here the folding kinetics of 18 variants of yACBP and
3 variants of bACBP have been studied by Phi-value analysis. In combination with
Phi-values from previous work, detailed insight into the transition states for
folding of both yACBP and bACBP has been obtained. Of the 16 sequence positions
that have been studied in both yACBP and bACBP, 5 (V12, I/L27, Y73, V77, and
L80) have high Phi-values and appear to be important for the transition state
formation in both homologues. Y31, A34, and A69 have high Phi-values only in
yACBP, while F5, A9, and I74 have high Phi-values only in bACBP. Thus,
additional interactions between helices A2 and A4 appear to be important for the
transition state of yACBP, whereas additional interactions between helices A1
and A4 appear to be important for the transition state of bACBP. To examine
whether these differences could be assigned to different packing of the residues
in the native state, a solution structure of yACBP was determined by NMR. Small
changes in the packing of the hydrophobic side-chains, which strengthen the
interactions between helices A2 and A4, are observed in yACBP relative to bACBP.
It is suggested that different structure elements serve as scaffolds for the
folding of the 2 ACBP homologues.
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Selected figure(s)
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Figure 5.
Figure 5. Effect of changes in  G[UN]
on  [U]
(top panel) and on m[eq,kin] (  ),
m[u] (  ),
and m[f] (  linear
fits, and the dotted lines are 95% prediction limits for the
fits.
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Figure 8.
Figure 8.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
59,
80-90)
copyright 2005.
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Figures were
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.A.Nickson,
and
J.Clarke
(2010).
What lessons can be learned from studying the folding of homologous proteins?
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Methods,
52,
38-50.
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S.W.Bruun,
V.Iesmantavicius,
J.Danielsson,
and
F.M.Poulsen
(2010).
Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein.
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Proc Natl Acad Sci U S A,
107,
13306-13311.
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A.Steward,
G.S.McDowell,
and
J.Clarke
(2009).
Topology is the principal determinant in the folding of a complex all-alpha Greek key death domain from human FADD.
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J Mol Biol,
389,
425-437.
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K.Teilum,
J.G.Olsen,
and
B.B.Kragelund
(2009).
Functional aspects of protein flexibility.
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Cell Mol Life Sci,
66,
2231-2247.
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G.Morra,
and
G.Colombo
(2008).
Relationship between energy distribution and fold stability: Insights from molecular dynamics simulations of native and mutant proteins.
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Proteins,
72,
660-672.
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K.Teilum,
F.M.Poulsen,
and
M.Akke
(2006).
The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein.
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Proc Natl Acad Sci U S A,
103,
6877-6882.
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M.D.Costabel,
M.R.Ermácora,
J.A.Santomé,
P.M.Alzari,
and
D.M.Guérin
(2006).
Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
958-961.
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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
