ArticleActa crystallographica. Section D, Biological crystallography2011
Streptavidin and its biotin complex at atomic resolution.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Liposomal nanoprobes actuated by engineered water channels for sensitive detection of molecular targets by MRI.Nature biomedical engineering · 2026Article
- Brownian Motion Paving the Way for Molecular Translocation in Nanopores.Small methods · 2024Article
- Design and Construction of a Multi-Tiered Minimal Actin Cortex for Structural Support in Lipid Bilayer Applications.ACS applied bio materials · 2024Article
- Kinetic study of membrane protein interactions: from three to two dimensions.Scientific reports · 2024Article
- Mapping Single-Molecule Protein Complexes in 3D with DNA Nanoswitch Calipers.Journal of the American Chemical Society · 2023Article
- Supramolecular Click Chemistry for Surface Modification of Quantum Dots Mediated by Cucurbit[7]uril.ACS nano · 2023Article
- An Analysis of the Biotin-(Strept)avidin System in Immunoassays: Interference and Mitigation Strategies.Current issues in molecular biology · 2023Review
- Article
- Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding.The journal of physical chemistry. B · 2023Article
- Sortase A transpeptidation produces seamless, unbranched biotinylated nanobodies for multivalent and multifunctional applications.Nanoscale advances · 2023Article
- Error-Correction Method for High-Throughput Sizing of Nanoscale Vesicles with Single-Molecule Localization Microscopy.The journal of physical chemistry. B · 2023Article
- Review
- Assessing models of force-dependent unbinding rates via infrequent metadynamics.The Journal of chemical physics · 2022Article
- A Strategy to Select Macrocyclic Peptides Featuring Asymmetric Molecular Scaffolds as Cyclization Units by Phage Display.Journal of the American Chemical Society · 2022Article
- Atomistic Simulations of Functionalized Nano-Materials for Biosensors Applications.International journal of molecular sciences · 2022Review
- Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature.Communications biology · 2022Article
- Tuning gold-based surface functionalization for streptavidin detection: A combined simulative and experimental study.Frontiers in molecular biosciences · 2022Article
- Streptavidin Coverage on Biotinylated Surfaces.ACS applied materials & interfaces · 2021Article
- Structural Origins of Altered Spectroscopic Properties upon Ligand Binding in Proteins Containing a Fluorescent Noncanonical Amino Acid.Biochemistry · 2021Article
- Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.Acta crystallographica. Section F, Structural biology communications · 2021Article
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Authors and funding
6 authors.
Funding
Abstract
Atomic resolution crystallographic studies of streptavidin and its biotin complex have been carried out at 1.03 and 0.95 Å, respectively. The wild-type protein crystallized with a tetramer in the asymmetric unit, while the crystals of the biotin complex contained two subunits in the asymmetric unit. Comparison of the six subunits shows the various ways in which the protein accommodates ligand binding and different crystal-packing environments. Conformational variation is found in each of the polypeptide loops connecting the eight strands in the β-sandwich subunit, but the largest differences are found in the flexible binding loop (residues 45-52). In three of the unliganded subunits the loop is in an `open' conformation, while in the two subunits binding biotin, as well as in one of the unliganded subunits, this loop `closes' over the biotin-binding site. The `closed' loop contributes to the protein's high affinity for biotin. Analysis of the anisotropic displacement parameters included in the crystallographic models is consistent with the variation found in the loop structures and the view that the dynamic nature of the protein structure contributes to the ability of the protein to bind biotin so tightly.
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