2CW1
Solution structure of the de novo-designed lambda Cro fold protein
Summary for 2CW1
| Entry DOI | 10.2210/pdb2cw1/pdb |
| Descriptor | SN4m (1 entity in total) |
| Functional Keywords | lambda cro fold, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 7488.70 |
| Authors | Isogai, Y.,Ito, Y.,Ikeya, T.,Shiro, Y.,Ota, M. (deposition date: 2005-06-15, release date: 2005-12-13, Last modification date: 2024-05-29) |
| Primary citation | Isogai, Y.,Ito, Y.,Ikeya, T.,Shiro, Y.,Ota, M. Design of lambda Cro fold: solution structure of a monomeric variant of the de novo protein. J.Mol.Biol., 354:801-814, 2005 Cited by PubMed Abstract: One of the classical DNA-binding proteins, bacteriophage lambda Cro, forms a homodimer with a unique fold of alpha-helices and beta-sheets. We have computationally designed an artificial sequence of 60 amino acid residues to stabilize the backbone tertiary structure of the lambda Cro dimer by simulated annealing using knowledge-based structure-sequence compatibility functions. The designed amino acid sequence has 25% identity with that of natural lambda Cro and preserves Phe58, which is important for formation of the stably folded structure of lambda Cro. The designed dimer protein and its monomeric variant, which was redesigned by the insertion of a beta-hairpin sequence at the C-terminal region to prevent dimerization, were synthesized and biochemically characterized to be well folded. The designed protein was monomeric under a wide range of protein concentrations and its solution structure was determined by NMR spectroscopy. The solved structure is similar to that of a monomeric variant of natural lambda Cro with a root-mean-square deviation of the polypeptide backbones at 2.1A and has a well-packed protein core. Thus, our knowledge-based functions provide approximate but essential relationships between amino acid sequences and protein structures, and are useful for finding novel sequences that are foldable into a given target structure. PubMed: 16289118DOI: 10.1016/j.jmb.2005.10.005 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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