1RPO
RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE
Summary for 1RPO
| Entry DOI | 10.2210/pdb1rpo/pdb |
| Descriptor | ROP PROTEIN (2 entities in total) |
| Functional Keywords | transcription regulation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 7379.19 |
| Authors | Vlassi, M.,Kokkinidis, M. (deposition date: 1994-08-25, release date: 1995-02-14, Last modification date: 2024-02-14) |
| Primary citation | Vlassi, M.,Steif, C.,Weber, P.,Tsernoglou, D.,Wilson, K.S.,Hinz, H.J.,Kokkinidis, M. Restored heptad pattern continuity does not alter the folding of a four-alpha-helix bundle. Nat.Struct.Biol., 1:706-716, 1994 Cited by PubMed Abstract: The sequences of alpha-helical coiled-coils and bundles are characterized by a specific pattern of hydrophobic and hydrophilic residues which is repeated every seven residues. Highly conserved breaks in this pattern frequently occur in segments of otherwise continuous heptad substructures. The hairpin bend of the ROP protein coincides with such a break and provides a model system for the study of the structural effects induced by heptad discontinuities. The structure of a ROP mutant which re-establishes a continuous heptad pattern, shows insignificant changes relative to the wild-type protein, as is also reflected in its conformational stability, spectroscopic properties and unfolding behaviour. Thus, formation of alpha-alpha-hairpin bends may occur both in the presence and absence of heptad breaks. PubMed: 7634075DOI: 10.1038/nsb1094-706 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
