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PDBsum entry 4do2
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RNA binding protein
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PDB id
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4do2
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References listed in PDB file
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Key reference
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Title
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Structural plasticity of 4-α-Helical bundles exemplified by the puzzle-Like molecular assembly of the rop protein.
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Authors
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M.Amprazi,
D.Kotsifaki,
M.Providaki,
E.G.Kapetaniou,
G.Fellas,
I.Kyriazidis,
J.Pérez,
M.Kokkinidis.
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Ref.
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Proc Natl Acad Sci U S A, 2014,
111,
11049-11054.
[DOI no: ]
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PubMed id
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Abstract
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The dimeric Repressor of Primer (Rop) protein, a widely used model system for
the study of coiled-coil 4-α-helical bundles, is characterized by a remarkable
structural plasticity. Loop region mutations lead to a wide range of topologies,
folding states, and altered physicochemical properties. A protein-folding study
of Rop and several loop variants has identified specific residues and sequences
that are linked to the observed structural plasticity. Apart from the native
state, native-like and molten-globule states have been identified; these states
are sensitive to reducing agents due to the formation of nonnative disulfide
bridges. Pro residues in the loop are critical for the establishment of new
topologies and molten globule states; their effects, however, can be in part
compensated by Gly residues. The extreme plasticity in the assembly of
4-α-helical bundles reflects the capacity of the Rop sequence to combine a
specific set of hydrophobic residues into strikingly different hydrophobic
cores. These cores include highly hydrated ones that are consistent with the
formation of interchain, nonnative disulfide bridges and the establishment of
molten globules. Potential applications of this structural plasticity are among
others in the engineering of bio-inspired materials.
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Secondary reference #1
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Title
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Purification, Crystallization and preliminary X-Ray diffraction analysis of a variant of the cole1 rop protein.
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Authors
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M.Ambrazi,
G.Fellas,
E.G.Kapetaniou,
D.Kotsifaki,
M.Providaki,
M.Kokkinidis.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
432-434.
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PubMed id
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