Cooperative Allostery and Structural Dynamics of Streptavidin at Cryogenic- and Ambient-temperature

• DOI: 10.1101/2021.09.23.461567
• Publication Date: 2021-09-24T14:30:37Z
• Authors: Esra Ayan; Busra Yuksel; Ebru Destan; Fatma Betul Ertem; Gunseli Yildirim; Meryem Eren; Oleksandr M. Yefanov; Anton Barty; Alexandra Tolstikova; Gihan K. Ketawala; Sabine Botha; E. Han Dao; Brandon Hayes; Mengning Liang; Matthew H. Seaberg; Mark S. Hunter; Alex Batyuk; Valerio Mariani; Zhen Su; Frederic Poitevin; Chun Hong Yoon; Christopher Kupitz; Aina Cohen; Tzanko Doukov; Raymond G. Sierra; Çağdaş Dağ; Hasan DeMirci
• Keywords: 0301 basic medicine; Artificial intelligence; Biology; Multidisciplinary sciences; Biochemistry; Streptavidin; Temperature; Materials Chemistry; Nanotechnology; Biology (General); info:eu-repo/classification/ddc/570; 0303 health sciences; Crystallography; Ecology; Physics; Temperature; Life Sciences; Allosteric regulation; Atomic and Molecular Physics, and Optics; Chemistry; Atomic Force Microscopy Techniques; Physical Sciences; Structural biology; 570; QH301-705.5; Chemical physics; Materials Science; Femtosecond; Biophysics; Biotin; Laser; Multidisciplinary sciences; Article; 03 medical and health sciences; Biochemistry, Genetics and Molecular Biology; Proximity-Dependent Protein Labeling in Living Cells; Biology; FOS: Nanotechnology; Macromolecular Crystallography Techniques; Optics; Cell Biology; Computer science; Materials science; Resolution (logic); Physics and Astronomy; Enzyme; FOS: Biological sciences; Crystal Structure Determination; Streptavidin; Substrate (aquarium)

ABSTRACTMultimeric protein assemblies are abundant in nature. Streptavidin is an attractive protein that provides a paradigm system to investigate the intra- and intermolecular interactions of multimeric protein complexes. Also, it offers a versatile tool for biotechnological applications. Here, we present two apo-streptavidin structures, the first one is an ambient temperature Serial Femtosecond X-ray crystal (Apo-SFX) structure at 1.7 Å resolution and the second one is a cryogenic crystal structure (Apo-Cryo) at 1.1 Å resolution. These structures are mostly in agreement with previous structural data. Combined with computational analysis, these structures provide invaluable information about structural dynamics of apo streptavidin. Collectively, these data further reveal a novel cooperative allostery of streptavidin which binds to substrate via water molecules that provide a polar interaction network and mimics the substrate biotin which displays one of the strongest affinities found in nature.