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

By Esra Ayan, Busra Yuksel, Ebru Destan, Fatma Betul Ertem, Gunseli Yildirim, Meryem Eren, Oleksandr M. Yefanov, Anton Barty, Alexandra Tolstikova, Gihan Kaushylal Ketawala1, Sabine Botha1, E. Han Dao, Brandon Hayes2, Mengning Liang, Matthew H. Seaberg, Mark S. Hunter2, Alexander Batyuk, Valerio Mariani, Zhen Su, Frederic Poitevin, Chun Hong Yoon, Christopher Kupitz2, Aina Cohen, Tzanko Doukov, Raymond G. Sierra, Çağdaş Dağ, Hasan Demirci3

1. Arizona State University 2. SLAC National Accelerator Laboratory 3. Biosciences Division at SLAC National Accelerator Laboratory

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

Esra Ayan and Busra Yuksel and Ebru Destan and Fatma Betul Ertem and Gunseli Yildirim and Meryem Eren and Oleksandr M. Yefanov and Anton Barty and Alexandra Tolstikova and Gihan K. Ketawala and Sabine Botha and E. Han Dao and Brandon Hayes and Mengning Liang and Matthew H. Seaberg and Mark S. Hunter and Alexander Batyuk and Valerio Mariani and Zhen Su and Frederic Poitevin and Chun Hong Yoon and Christopher Kupitz and Aina Cohen and Tzanko Doukov and Raymond G. Sierra and Çağdaş Dağ and Hasan DeMirci

Citation

Ayan, E., Yuksel, B., Destan, E., Ertem, F. B., Yildirim, G., Eren, M., Yefanov, O. M., Barty, A., Tolstikova, A., Ketawala, G. K., Botha, S., Dao, E. H., Hayes, B., Liang, M., Seaberg, M. H., Hunter, M. S., Batyuk, A., Mariani, V., Su, Z., … DeMirci, H. (2022). Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature. Communications Biology, 5(1). https://doi.org/10.1038/s42003-021-02903-7

Abstract

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.

DOI

http://dx.doi.org/10.1038/s42003-021-02903-7