2ON8
Gbeta1 stabilization by in vitro evolution and computational design
Summary for 2ON8
| Entry DOI | 10.2210/pdb2on8/pdb |
| Related | 1FCC 1GB4 1P7E 1PGA 1PGB 3GB1 |
| Descriptor | Immunoglobulin G-binding protein G (2 entities in total) |
| Functional Keywords | beta sheet, alpha helix, improved hydrophobic packing of core residues, protein binding |
| Biological source | Streptococcus sp. |
| Cellular location | Secreted, cell wall ; Peptidoglycan-anchor : P19909 |
| Total number of polymer chains | 1 |
| Total formula weight | 6309.00 |
| Authors | Max, K.E.A.,Heinemann, U. (deposition date: 2007-01-23, release date: 2007-12-04, Last modification date: 2023-08-30) |
| Primary citation | Wunderlich, M.,Max, K.E.,Roske, Y.,Mueller, U.,Heinemann, U.,Schmid, F.X. Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization. J.Mol.Biol., 373:775-784, 2007 Cited by PubMed Abstract: Computational design and in vitro evolution are major strategies for stabilizing proteins. For the four critical positions 16, 18, 25, and 29 of the B domain of the streptococcal protein G (Gbeta1), they identified the same optimal residues at positions 16 and 25, but not at 18 and 29. Here we analyzed the energetic contributions of the residues from these two approaches by single and double mutant analyses and determined crystal structures for a variant from the calculation (I16/L18/E25/K29) and from the selection (I16/I18/E25/F29). The structural analysis explains the observed differences in stabilization. Residues 16, 18, and 29 line an invagination, which results from a packing defect between the helix and the beta-sheet of Gbeta1. In all stabilized variants, residues with larger side-chains occur at these positions and packing is improved. In the selected variant, packing is better optimized than in the computed variant. Such differences in side-chain packing strongly affect stability but are difficult to evaluate by computation. PubMed: 17868696DOI: 10.1016/j.jmb.2007.08.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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