Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature
Esra Ayan, Büşra Yüksel, Ebru Destan, Fatma Betül Ertem, Günseli Yıldırım, Meryem Eren, Oleksandr Yefanov, Anton Barty, A. Tolstikova, Gihan Ketawala, Sabine Botha, E. Han Dao, Brandon Hayes, Mengning Liang, Matthew Seaberg, Mark S. Hunter, A. Batyuk, Valerio Mariani, Zhen Su, Frédéric Poitevin, Chun Hong Yoon, Christopher Kupitz, Aina E. Cohen, Tzanko Doukov, Raymond G. Sierra, Çağdaş Dağ, Hasan DeMi̇rci̇
Abstract
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.