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PDBsum entry 1quu
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Contractile protein
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PDB id
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1quu
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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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Structure of the alpha-Actinin rod: molecular basis for cross-Linking of actin filaments.
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Authors
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K.Djinović-Carugo,
P.Young,
M.Gautel,
M.Saraste.
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Ref.
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Cell, 1999,
98,
537-546.
[DOI no: ]
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PubMed id
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Abstract
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We have determined the crystal structure of the two central repeats in the
alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical
linker and form a symmetric, antiparallel dimer in which the repeats are aligned
rather than staggered. Using this structure, which reveals the structural
principle that governs the architecture of alpha-actinin, we have devised a
plausible model of the entire alpha-actinin rod. The electrostatic properties
explain how the two alpha-actinin subunits assemble in an antiparallel fashion,
placing the actin-binding sites at both ends of the rod. This molecular
architecture results in a protein that is able to form cross-links between actin
filaments.
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Figure 3.
Figure 3. The Connecting LinkerClose-up of interactions
between R2, R3, and the linker. The protein backbone is shown as
a ribbon, and amino acid residues are drawn in a ball-and-stick
representation. R2 is colored blue, R3 is green, and the linker
is red.
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Figure 6.
Figure 6. Model of the α-Actinin Rod(A) Sequence alignment
of the α-actinin repeats used in modeling of repeats R1 and R4.
Residue numbers for the full-length molecule and those of the
construct used for the crystal structure are indicated at the
edges and above the alignment, respectively. The α helices
seen in the crystal structure are depicted as bars (blue for R2
and green for R3). The C termini of R1 and R3 and the N termini
of R2 and R4, respectively, overlap due to the modeling
procedure of R1 and R4. The overlapping residues shown in italic
were used to assemble the model of the rod. The figure was
generated with ALSCRIPT ([1]).(B) Ribbon diagram of α-actinin
rod viewed in two orientations related by a 65 degree rotation
around the long molecular axis through the central 2-fold axis.
R1 is colored violet, R2 is blue, R3 is green, and R4 is
yellow.(C) Electrostatic surface potential of one R1–R4
subunit generated with GRASP ([38]). Positively charged surface
is colored blue and negatively charged red. The second subunit
is white in a wormlike representation. Surfaces corresponding to
R1 and R4 are marked.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1999,
98,
537-546)
copyright 1999.
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