Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature

• Published in: Communications biology Vol. 5; no. 1; p. 73
• Main Authors: Ayan, Esra, Yuksel, Busra, Destan, Ebru, Ertem, Fatma Betul, Yildirim, Gunseli, Eren, Meryem, Yefanov, Oleksandr M, Barty, Anton, Tolstikova, Alexandra, Ketawala, Gihan K, Botha, Sabine, Dao, E Han, Hayes, Brandon, Liang, Mengning, Seaberg, Matthew H, Hunter, Mark S, Batyuk, Alexander, Mariani, Valerio, Su, Zhen, Poitevin, Frederic, Yoon, Chun Hong, Kupitz, Christopher, Cohen, Aina, Doukov, Tzanko, Sierra, Raymond G, Dağ, Çağdaş, DeMirci, Hasan
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 20.01.2022; Springer Nature; Nature Publishing Group UK; Nature Portfolio
• Subjects: 60 APPLIED LIFE SCIENCES; Biology; Biotin; Computer applications; Crystal structure; Crystallography; Monomers; Proteins; Serial Femtosecond X-ray Crystallography; Streptavidin; Streptavidin - ultrastructure; Temperature
• ISSN: 2399-3642; 2399-3642
• DOI: 10.1038/s42003-021-02903-7

Multimeric 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.