3MG5
Core-streptavidin mutant F130L in complex with biotin
Summary for 3MG5
| Entry DOI | 10.2210/pdb3mg5/pdb |
| Related | 1MK5 |
| Descriptor | Streptavidin, BIOTIN, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | biotin-binding protein, streptavidin |
| Biological source | Streptomyces avidinii |
| Cellular location | Secreted: P22629 |
| Total number of polymer chains | 4 |
| Total formula weight | 54979.55 |
| Authors | Le Trong, I.,Baugh, L.,Stayton, P.S.,Lybrand, T.P.,Stenkamp, R.E. (deposition date: 2010-04-05, release date: 2010-05-26, Last modification date: 2023-09-06) |
| Primary citation | Baugh, L.,Le Trong, I.,Cerutti, D.S.,Gulich, S.,Stayton, P.S.,Stenkamp, R.E.,Lybrand, T.P. A distal point mutation in the streptavidin-biotin complex preserves structure but diminishes binding affinity: experimental evidence of electronic polarization effects? Biochemistry, 49:4568-4570, 2010 Cited by PubMed Abstract: We have identified a distal point mutation in streptavidin that causes a 1000-fold reduction in biotin binding affinity without disrupting the equilibrium complex structure. The F130L mutation creates a small cavity occupied by a water molecule; however, all neighboring side chain positions are preserved, and protein-biotin hydrogen bonds are unperturbed. Molecular dynamics simulations reveal a reduced mobility of biotin binding residues but no observable destabilization of protein-ligand interactions. Our combined structural and computational studies suggest that the additional water molecule may affect binding affinity through an electronic polarization effect that impacts the highly cooperative hydrogen bonding network in the biotin binding pocket. PubMed: 20462252DOI: 10.1021/bi1005392 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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