Structural Basis of Oligomerization of N-Terminal Domain of Spider Aciniform Silk Protein
| Autor: | Palur Venkata Raghuvamsi, Ganesh S. Anand, Daiwen Yang, Chong Cheong Lai, Jing-Song Fan, Pin Xuan Chee, Rusha Chakraborty |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Protein Conformation Dimer Sequence Homology 01 natural sciences lcsh:Chemistry chemistry.chemical_compound Protein structure Spider silk lcsh:QH301-705.5 Spectroscopy NMR spider spectroscopy Spiders General Medicine Nuclear magnetic resonance spectroscopy Hydrogen-Ion Concentration spider silk protein Computer Science Applications Monomer SILK Insect Proteins Nephila antipodiana Silk protein oligomerization macromolecular substances 010402 general chemistry silk formation Article Catalysis Inorganic Chemistry 03 medical and health sciences Protein Domains Animals Protein oligomerization Amino Acid Sequence protein structure Physical and Theoretical Chemistry Molecular Biology fungi Organic Chemistry technology industry and agriculture protein self-assembly equipment and supplies 0104 chemical sciences 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 chemistry Biophysics Protein Multimerization |
| Zdroj: | International Journal of Molecular Sciences, Vol 21, Iss 4466, p 4466 (2020) International Journal of Molecular Sciences Volume 21 Issue 12 |
| ISSN: | 1422-0067 |
| Popis: | Spider silk is self-assembled from water-soluble silk proteins through changes in the environment, including pH, salt concentrations, and shear force. The N-terminal domains of major and minor ampullate silk proteins have been found to play an important role in the assembly process through salt- and pH-dependent dimerization. Here, we identified the sequences of the N-terminal domains of aciniform silk protein (AcSpN) and major ampullate silk protein (MaSpN) from Nephila antipodiana (NA). Different from MaSpN, our biophysical characterization indicated that AcSpN assembles to form large oligomers, instead of a dimer, upon condition changes from neutral to acidic pH and/or from a high to low salt concentration. Our structural studies, by nuclear magnetic resonance spectroscopy and homology modelling, revealed that AcSpN and MaSpN monomers adopt similar overall structures, but have very different charge distributions contributing to the differential self-association features. The intermolecular interaction interfaces for AcSp oligomers were identified using hydrogen&ndash deuterium exchange mass spectrometry and mutagenesis. On the basis of the monomeric structure and identified interfaces, the oligomeric structures of AcSpN were modelled. The structural information obtained will facilitate an understanding of silk fiber formation mechanisms for aciniform silk protein. |
| Databáze: | OpenAIRE |
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