2RU5

Designed Armadillo Repeat Protein Fragment (MAII)

Summary for 2RU5

• Entry DOI: 10.2210/pdb2ru5/pdb
• Related: 2ru4
• NMR Information: BMRB: 11548
• Descriptor: Armadillo repeat protein C-terminal fragment (1 entity in total)
• Functional Keywords: solenoid repeat, armadillo repeat motif, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 9104.07

Authors

Zerbe, O.,Christen, M.T.,Plueckthun, A.,Watson, R.P. (deposition date: 2013-11-23, 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

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: 24931467
DOI: 10.1016/j.str.2014.05.002

Experimental method

SOLUTION NMR