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PDBsum entry 2b22
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Biosynthetic protein
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PDB id
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2b22
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DOI no:
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Structure
14:247-255
(2006)
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PubMed id:
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Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat.
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Y.Deng,
J.Liu,
Q.Zheng,
D.Eliezer,
N.R.Kallenbach,
M.Lu.
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ABSTRACT
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Coiled-coil sequences in proteins commonly share a seven-amino acid repeat with
nonpolar side chains at the first (a) and fourth (d) positions. We investigate
here the role of a 3-3-1 hydrophobic repeat containing nonpolar amino acids at
the a, d, and g positions in determining the structures of coiled coils using
mutants of the GCN4 leucine zipper dimerization domain. When three charged
residues at the g positions in the parental sequence are replaced by nonpolar
alanine or valine side chains, stable four-helix structures result. The X-ray
crystal structures of the tetramers reveal antiparallel, four-stranded coiled
coils in which the a, d, and g side chains interlock in a combination of
knobs-into-knobs and knobs-into-holes packing. Interfacial interactions in a
coiled coil can therefore be prescribed by hydrophobic-polar patterns beyond the
canonical 3-4 heptad repeat. The results suggest that the conserved, charged
residues at the g positions in the GCN4 leucine zipper can impart a negative
design element to disfavor thermodynamically more stable, antiparallel tetramers.
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Selected figure(s)
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Figure 3.
Figure 3. Crystal Structure of the GCN4-pA Tetramer (A)
Lateral view of the tetramer. Red van der Waals surfaces
identify residues at the a positions, green surfaces identify
residues at the d positions, and yellow surfaces identify
residues at the g positions. The N termini of helices A and B
are indicated. (B) Axial view of the tetramer. The green,
yellow, and red van der Waals surfaces of the L6 (d), L30 (g),
and V31 (a) side chains are depicted. (C) Cross-section of
the superhelix in the L20 (d) layer. The 1.5 Å 2F[o] –
F[c] electron density map (contoured at 1.5σ) is shown with the
refined molecular model. (D) Helical wheel projection of
residues 2–32 of the GCN4-pA tetramer. Heptad repeat positions
are labeled a–g. The leucines at the d positions form the
apolar interface of the tetramer.
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Figure 4.
Figure 4. Crystal Structure of the GCN4-pV Tetramer (A)
Lateral view of the tetramer. Red van der Waals surfaces
identify residues at the a positions, green surfaces identify
residues at the d positions, and yellow surfaces identify
residues at the g positions. The N termini of helices A and B
are indicated. (B) Axial view of the tetramer. The green,
yellow, and red van der Waals surfaces of the L6 (d), L30 (g),
and V31 (a) side chains are depicted. (C) Cross-section of
the superhelix in the L20 (d) layer. The 2F[o] – F[c] electron
density map at 1.2σ contour is shown with the refined molecular
model. (D) Superposition of the backbone conformations of
the parallel GCN4-pIL tetramer (red) and the antiparallel
GCN4-pA (green) and GCN4-pV (yellow) tetramers.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(2006,
14,
247-255)
copyright 2006.
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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.Giamarchi,
S.Feng,
L.Rodat-Despoix,
Y.Xu,
E.Bubenshchikova,
L.J.Newby,
J.Hao,
C.Gaudioso,
M.Crest,
A.N.Lupas,
E.Honoré,
M.P.Williamson,
T.Obara,
A.C.Ong,
and
P.Delmas
(2010).
A polycystin-2 (TRPP2) dimerization domain essential for the function of heteromeric polycystin complexes.
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EMBO J,
29,
1176-1191.
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J.Diao
(2010).
Crystal structure of a super leucine zipper, an extended two-stranded super long coiled coil.
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Protein Sci,
19,
319-326.
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PDB code:
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S.Banta,
I.R.Wheeldon,
and
M.Blenner
(2010).
Protein engineering in the development of functional hydrogels.
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Annu Rev Biomed Eng,
12,
167-186.
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D.Albanesi,
M.Martín,
F.Trajtenberg,
M.C.Mansilla,
A.Haouz,
P.M.Alzari,
D.de Mendoza,
and
A.Buschiazzo
(2009).
Structural plasticity and catalysis regulation of a thermosensor histidine kinase.
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Proc Natl Acad Sci U S A,
106,
16185-16190.
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PDB codes:
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A.Surcel,
D.Koshland,
H.Ma,
and
R.T.Simpson
(2008).
Cohesin interaction with centromeric minichromosomes shows a multi-complex rod-shaped structure.
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PLoS ONE,
3,
e2453.
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D.N.Ho,
N.C.Pomroy,
J.A.Cuesta-Seijo,
and
G.G.Privé
(2008).
Crystal structure of a self-assembling lipopeptide detergent at 1.20 A.
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Proc Natl Acad Sci U S A,
105,
12861-12866.
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PDB code:
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G.Grigoryan,
and
A.E.Keating
(2008).
Structural specificity in coiled-coil interactions.
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Curr Opin Struct Biol,
18,
477-483.
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Y.Fujiwara,
and
D.L.Minor
(2008).
X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil.
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J Mol Biol,
383,
854-870.
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PDB code:
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Y.Deng,
Q.Zheng,
J.Liu,
C.S.Cheng,
N.R.Kallenbach,
and
M.Lu
(2007).
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.
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Protein Sci,
16,
323-328.
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PDB code:
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M.Hulko,
F.Berndt,
M.Gruber,
J.U.Linder,
V.Truffault,
A.Schultz,
J.Martin,
J.E.Schultz,
A.N.Lupas,
and
M.Coles
(2006).
The HAMP domain structure implies helix rotation in transmembrane signaling.
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Cell,
126,
929-940.
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Y.Deng,
J.Liu,
Q.Zheng,
W.Yong,
and
M.Lu
(2006).
Structures and polymorphic interactions of two heptad-repeat regions of the SARS virus S2 protein.
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Structure,
14,
889-899.
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PDB codes:
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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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}
}
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