3t6l | pdb_00003t6l

Y54F mutant of core streptavidin

spinqualitylabelsall models 3t6l, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3t6l is a 1 chain structure with sequence from As 4.1583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EDO Related: 3t6f Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMed We report a point mutation in the second contact shell of the high-affinity streptavidin-biotin complex that appears to reduce binding affinity through transmitted effects on equilibrium dynamics. The Y54F streptavidin mutation causes a 75-fold loss of binding affinity with 73-fold faster dissociation, a large loss of binding enthalpy (DeltaDeltaH, 3.4 kcal/mol at 37 masculineC) and a small gain in binding entropy (TDeltaDeltaS, 0.7 kcal/mol). The removed Y54 hydroxyl is replaced by a water molecule in the bound structure, but there are no observable changes in structure in the first contact shell and no additional changes surrounding the mutation. Molecular dynamics simulations reveal a large increase in atomic fluctuations for W79, a key biotin contact residue, compared to the wild type complex. The increased W79 fluctuations are caused by loss of water-mediated hydrogen bonds between the Y54 hydroxyl group and peptide backbone atoms in and near W79. We propose that the increased fluctuations diminish the integrity of the W79-biotin interaction and represent a loosening of the "tryptophan collar" which is critical to the slow dissociation and high affinity of streptavidin-biotin binding. These results illustrate how changes in protein dynamics distal to the ligand binding pocket can have a profound impact on ligand binding, even when equilibrium structure is unperturbed. Second Contact Shell Mutation Diminishes Streptavidin-Biotin Binding Affinity Through Transmitted Effects on Equilibrium Dynamics.,Baugh L, Le Trong I, Cerutti DS, Mehta N, Gulich S, Stayton PS, Stenkamp RE, Lybrand TP Biochemistry. 2011 Dec 6. PMID:22145986 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin 3D structures

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