4DO2
Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.
Summary for 4DO2
| Entry DOI | 10.2210/pdb4do2/pdb |
| Related | 1ROP |
| Descriptor | Regulatory protein rop (2 entities in total) |
| Functional Keywords | protein structure, protein folding, rop protein, bacterial protein, mutation, 4-alpha-helical bundle, loop, rna binding protein, cole1 plasmid copy number |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 16326.07 |
| Authors | Amprazi, M.,Kapetaniou, E.G.,Kokkinidis, M. (deposition date: 2012-02-09, release date: 2013-02-13, Last modification date: 2023-09-13) |
| Primary citation | Amprazi, M.,Kotsifaki, D.,Providaki, M.,Kapetaniou, E.G.,Fellas, G.,Kyriazidis, I.,Perez, J.,Kokkinidis, M. Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein. Proc.Natl.Acad.Sci.USA, 111:11049-11054, 2014 Cited by PubMed Abstract: 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. PubMed: 25024213DOI: 10.1073/pnas.1322065111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.401 Å) |
Structure validation
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