Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature.
Esra AyanBusra YukselEbru DestanFatma Betul ErtemGunseli YildirimMeryem ErenOleksandr M YefanovAnton BartyAlexandra TolstikovaGihan K KetawalaSabine BothaE Han DaoBrandon HayesMengning LiangMatthew H SeabergMark S HunterAlexander BatyukValerio MarianiZhen SuFrederic PoitevinChun Hong YoonChristopher KupitzAina CohenTzanko I DoukovRaymond G SierraÇağdaş DağHasan DeMirciPublished in: Communications biology (2022)
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.
Keyphrases
- high resolution
- crystal structure
- amino acid
- air pollution
- protein protein
- particulate matter
- electron microscopy
- electronic health record
- binding protein
- single molecule
- big data
- genome wide
- small molecule
- computed tomography
- magnetic resonance
- health information
- data analysis
- dna methylation
- ionic liquid
- deep learning
- dual energy
- structural basis