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3RDU

Crystal structure of R7-2 streptavidin complexed with PEG

Summary for 3RDU
Entry DOI10.2210/pdb3rdu/pdb
Related3RDM 3RDO 3RDQ 3RDS 3RDX 3RE5 3RE6
DescriptorStreptavidin, GLYCEROL, PENTAETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywordsstreptavidin variants, improved desthiobiotin binding, opened loop destabilization, biotin binding protein
Biological sourceStreptomyces avidinii
Cellular locationSecreted: P22629
Total number of polymer chains1
Total formula weight16480.94
Authors
Malashkevich, V.N.,Magalhaes, M.,Czecster, C.M.,Guan, R.,Levy, M.,Almo, S.C. (deposition date: 2011-04-01, release date: 2011-07-06, Last modification date: 2023-09-13)
Primary citationMagalhaes, M.L.,Czekster, C.M.,Guan, R.,Malashkevich, V.N.,Almo, S.C.,Levy, M.
Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding.
Protein Sci., 20:1145-1154, 2011
Cited by
PubMed Abstract: We have performed a detailed analysis of streptavidin variants with altered specificity towards desthiobiotin. In addition to changes in key residues which widen the ligand binding pocket and accommodate the more structurally flexible desthiobiotin, the data revealed the role of a key, non-active site mutation at the base of the flexible loop (S52G) which slows dissociation of this ligand by approximately sevenfold. Our data suggest that this mutation results in the loss of a stabilizing contact which keeps this loop open and accessible in the absence of ligand. When this mutation was introduced into the wild-type protein, destabilization of the opened loop conferred a ∼10-fold decrease in both the on-rate and off-rate for the ligand biotin-4-fluoroscein. A similar effect was observed when this mutation was added to a monomeric form of this protein. Our results provide key insight into the role of the streptavidin flexible loop in ligand binding and maintaining high affinity interactions.
PubMed: 21520321
DOI: 10.1002/pro.642
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

226707

數據於2024-10-30公開中

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