Published January 1, 2022
| Version v1
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Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature
Creators
- Ayan, Esra1
- Yuksel, Busra1
- Destan, Ebru1
- Ertem, Fatma Betul1
- Yildirim, Gunseli1
- Eren, Meryem1
- Yefanov, Oleksandr M.2
- Barty, Anton2
- Tolstikova, Alexandra2
- Ketawala, Gihan K.
- Botha, Sabine
- Dao, E. Han3
- Hayes, Brandon4
- Liang, Mengning4
- Seaberg, Matthew H.4
- Hunter, Mark S.4
- Batyuk, Alexander4
- Mariani, Valerio4
- Su, Zhen
- Poitevin, Frederic4
- Poitevin, Frederic4
- 1. Koc Univ, Dept Mol Biol & Genet, TR-34450 Istanbul, Turkey
- 2. DESY, Notkestr 85, D-22607 Hamburg, Germany
- 3. SLAC Natl Lab, Stanford PULSE Inst, Menlo Pk, CA 94025 USA
- 4. SLAC Natl Accelerator Lab, Linac Coherent Light Source, 2575 Sand Hill Rd, Menlo Pk, CA 94025 USA
Description
Ayan et al. report two structures of the protein streptavidin - one at ambient temperature determined using serial femtosecond crystallography and a second one determined at cryogenic temperature. These results provide insights into the structural dynamics of apo streptavidin and reveal a cooperative allostery between monomers for binding to biotin, and the findings are supported by GNM analysis.
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