7WIO
NMR structure of N-terminal domain of Triconephila clavipes of major ampullate spidroin 1
Summary for 7WIO
| Entry DOI | 10.2210/pdb7wio/pdb |
| Descriptor | Major ampullate spidroin 1A (1 entity in total) |
| Functional Keywords | dragline spider silk, spider silk assembly, ph regulation, structural protein |
| Biological source | Trichonephila clavipes |
| Total number of polymer chains | 1 |
| Total formula weight | 14499.00 |
| Authors | Oktaviani, N.A.,Malay, A.D.,Matsugami, A.,Hayashi, F.,Numata, K. (deposition date: 2022-01-04, release date: 2023-03-15, Last modification date: 2024-05-15) |
| Primary citation | Oktaviani, N.A.,Malay, A.D.,Matsugami, A.,Hayashi, F.,Numata, K. Unusual p K a Values Mediate the Self-Assembly of Spider Dragline Silk Proteins. Biomacromolecules, 24:1604-1616, 2023 Cited by PubMed Abstract: Spider dragline silk is a remarkably tough biomaterial and composed primarily of spidroins MaSp1 and MaSp2. During fiber self-assembly, the spidroin N-terminal domains (NTDs) undergo rapid dimerization in response to a pH gradient. However, obtaining a detailed understanding of this mechanism has been hampered by a lack of direct evidence regarding the protonation states of key ionic residues. Here, we elucidated the solution structures of MaSp1 and MaSp2 NTDs from and determined the experimental pa values of conserved residues involved in dimerization using NMR. Surprisingly, we found that the Asp40 located on an acidic cluster protonates at an unusually high pH (∼6.5-7.1), suggesting the first step in the pH response. Then, protonation of Glu119 and Glu79 follows, with ps above their intrinsic values, contributing toward stable dimer formation. We propose that exploiting the atypical p values is a strategy to achieve tight spatiotemporal control of spider silk self-assembly. PubMed: 36990448DOI: 10.1021/acs.biomac.2c01344 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
