4GXP
Chimeric Family 1 beta-glucosidase made with non-contiguous SCHEMA
Summary for 4GXP
| Entry DOI | 10.2210/pdb4gxp/pdb |
| Related | 2WBG 3AHY |
| Descriptor | Beta-glucosidase Chimeric protein (2 entities in total) |
| Functional Keywords | chimeragenesis, protein recombination, eukaryotic-prokaryotic chimera, gh1, beta-glucosidase, hydrolase |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 3 |
| Total formula weight | 159078.90 |
| Authors | Smith, M.A.,Romero, P.A.,Wu, T.,Brustad, E.M.,Arnold, F.H. (deposition date: 2012-09-04, release date: 2013-01-09, Last modification date: 2024-02-28) |
| Primary citation | Smith, M.A.,Romero, P.A.,Wu, T.,Brustad, E.M.,Arnold, F.H. Chimeragenesis of distantly-related proteins by noncontiguous recombination. Protein Sci., 22:231-238, 2013 Cited by PubMed Abstract: We introduce a method for identifying elements of a protein structure that can be shuffled to make chimeric proteins from two or more homologous parents. Formulating recombination as a graph-partitioning problem allows us to identify noncontiguous segments of the sequence that should be inherited together in the progeny proteins. We demonstrate this noncontiguous recombination approach by constructing a chimera of β-glucosidases from two different kingdoms of life. Although the protein's alpha-beta barrel fold has no obvious subdomains for recombination, noncontiguous SCHEMA recombination generated a functional chimera that takes approximately half its structure from each parent. The X-ray crystal structure shows that the structural blocks that make up the chimera maintain the backbone conformations found in their respective parental structures. Although the chimera has lower β-glucosidase activity than the parent enzymes, the activity was easily recovered by directed evolution. This simple method, which does not rely on detailed atomic models, can be used to design chimeras that take structural, and functional, elements from distantly-related proteins. PubMed: 23225662DOI: 10.1002/pro.2202 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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