5BVL
Crystal structure of a de novo designed TIM-barrel
Summary for 5BVL
| Entry DOI | 10.2210/pdb5bvl/pdb |
| Descriptor | designed TIM barrel sTIM11 (2 entities in total) |
| Functional Keywords | tim-barrel, computational design, idealized scaffold, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 22896.45 |
| Authors | Feldmeier, K.,Hocker, B. (deposition date: 2015-06-05, release date: 2015-11-18, Last modification date: 2024-05-01) |
| Primary citation | Huang, P.S.,Feldmeier, K.,Parmeggiani, F.,Fernandez Velasco, D.A.,Hocker, B.,Baker, D. De novo design of a four-fold symmetric TIM-barrel protein with atomic-level accuracy. Nat.Chem.Biol., 12:29-34, 2016 Cited by PubMed Abstract: Despite efforts for over 25 years, de novo protein design has not succeeded in achieving the TIM-barrel fold. Here we describe the computational design of four-fold symmetrical (β/α)8 barrels guided by geometrical and chemical principles. Experimental characterization of 33 designs revealed the importance of side chain-backbone hydrogen bonds for defining the strand register between repeat units. The X-ray crystal structure of a designed thermostable 184-residue protein is nearly identical to that of the designed TIM-barrel model. PSI-BLAST searches do not identify sequence similarities to known TIM-barrel proteins, and sensitive profile-profile searches indicate that the design sequence is distant from other naturally occurring TIM-barrel superfamilies, suggesting that Nature has sampled only a subset of the sequence space available to the TIM-barrel fold. The ability to design TIM barrels de novo opens new possibilities for custom-made enzymes. PubMed: 26595462DOI: 10.1038/nchembio.1966 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.992 Å) |
Structure validation
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