3UA0
N-Terminal Domain of Bombyx mori Fibroin Mediates the Assembly of Silk in Response to pH Decrease
Summary for 3UA0
| Entry DOI | 10.2210/pdb3ua0/pdb |
| Descriptor | Fibroin heavy chain (1 entity in total) |
| Functional Keywords | the double-layered-sheets, fibroin folding initiation, protein fibril |
| Biological source | Bombyx mori (silk moth,silkworm) |
| Total number of polymer chains | 2 |
| Total formula weight | 30280.09 |
| Authors | He, Y.-X.,Zhang, N.-N.,Chen, B.-Y.,Li, W.-F.,Chen, Y.-X.,Zhou, C.-Z. (deposition date: 2011-10-20, release date: 2012-03-28, Last modification date: 2024-11-06) |
| Primary citation | He, Y.X.,Zhang, N.N.,Li, W.F.,Jia, N.,Chen, B.Y.,Zhou, K.,Zhang, J.,Chen, Y.,Zhou, C.Z. N-Terminal Domain of Bombyx mori Fibroin Mediates the Assembly of Silk in Response to pH Decrease. J.Mol.Biol., 418:197-207, 2012 Cited by PubMed Abstract: Fibroins serve as the major building blocks of silk fiber. As the major component of fibroin, the fibroin heavy chain is a considerably large protein comprising N-terminal and C-terminal hydrophilic domains and 12 highly repetitive Gly-Ala-rich regions flanked by internal hydrophilic blocks. Here, we show the crystal structure of the fibroin N-terminal domain (FibNT) at pH 4.7, revealing a remarkable double-layered anti-parallel β-sheet with each layer comprising two FibNT molecules entangled together. We also show that FibNT undergoes a pH-responsive conformational transition from random coil to β-sheets at around pH 6.0. Dynamic light scattering demonstrates that FibNT tends to oligomerize as pH decreases to 6.0, and electron microscopy reveals micelle-like oligomers. Our results are consistent with the micelle assembly model of silk fibroin and, more importantly, show that the N-terminal domain in itself has the capacity to form micelle-like structures in response to pH decrease. Structural and mutagenesis analyses further reveal the important role of conserved acidic residues clustered in FibNT, such as Glu56 and Asp100, in preventing premature β-sheet formation at neutral pH. Collectively, we suggest that FibNT functions as a pH-responsive self-assembly module that could prevent premature β-sheet formation at neutral pH yet could initiate fibroin assembly as pH decreases along the lumen of the posterior silk gland to the anterior silk gland. PubMed: 22387468DOI: 10.1016/j.jmb.2012.02.040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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