Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 30, Pages 11049-11054Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1322065111
Keywords
recurrent tertiary motifs; core packing; disulfide bonds; dimensionless Kratky plot
Categories
Funding
- European Union-Regional Potential Programme [316223]
- Greece-France Joint Technology Research Programmes
- SOLEIL synchrotron
- Greek Ministry of Education
- short-term European Molecular Biology Organization fellowship
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The dimeric Repressor of Primer (Rop) protein, a widely used model system for the study of coiled-coil 4-alpha-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-alpha-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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