2RU4
Designed Armadillo Repeat Protein Self-ASsembled Complex (YIIM2-MAII)
Summary for 2RU4
| Entry DOI | 10.2210/pdb2ru4/pdb |
| Related | 2RU5 |
| NMR Information | BMRB: 11544 |
| Descriptor | Armadillo Repeat Protein, N-terminal fragment, YIIM2, Armadillo Repeat Protein, C-terminal fragment, MAII (2 entities in total) |
| Functional Keywords | solenoid repeat, armadillo repeat motif, de novo protein, self-assembly, solution complex |
| Biological source | synthetic construct More |
| Total number of polymer chains | 2 |
| Total formula weight | 21297.59 |
| Authors | Zerbe, O.,Christen, M.T.,Plueckthun, A.,Watson, R.P. (deposition date: 2013-11-22, release date: 2014-07-23, Last modification date: 2024-05-15) |
| Primary citation | Watson, R.P.,Christen, M.T.,Ewald, C.,Bumbak, F.,Reichen, C.,Mihajlovic, M.,Schmidt, E.,Guntert, P.,Caflisch, A.,Pluckthun, A.,Zerbe, O. Spontaneous self-assembly of engineered armadillo repeat protein fragments into a folded structure Structure, 22:985-995, 2014 Cited by PubMed Abstract: Repeat proteins are built of modules, each of which constitutes a structural motif. We have investigated whether fragments of a designed consensus armadillo repeat protein (ArmRP) recognize each other. We examined a split ArmRP consisting of an N-capping repeat (denoted Y), three internal repeats (M), and a C-capping repeat (A). We demonstrate that the C-terminal MA fragment adopts a fold similar to the corresponding part of the entire protein. In contrast, the N-terminal YM2 fragment constitutes a molten globule. The two fragments form a 1:1 YM2:MA complex with a nanomolar dissociation constant essentially identical to the crystal structure of the continuous YM3A protein. Molecular dynamics simulations show that the complex is structurally stable over a 1 μs timescale and reveal the importance of hydrophobic contacts across the interface. We propose that the existence of a stable complex recapitulates possible intermediates in the early evolution of these repeat proteins. PubMed: 24931467DOI: 10.1016/j.str.2014.05.002 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
