2MAB

Untangling the Solution Structure of C-Terminal Domain of Aciniform Spidroin

Summary for 2MAB

• Entry DOI: 10.2210/pdb2mab/pdb
• NMR Information: BMRB: 19340
• Descriptor: ACINIFORM SPIDROIN (1 entity in total)
• Functional Keywords: c-terminal domain, spider silk protein, aciniform spidroin, structural protein
• Biological source: Nephila Antipodiana
• Total number of polymer chains: 2
• Total formula weight: 21774.41

Authors

Wang, S.,Yang, D. (deposition date: 2013-07-09, release date: 2014-03-05, Last modification date: 2024-05-15)

Primary citation

Wang, S.,Huang, W.,Yang, D.
Structure and function of C-terminal domain of aciniform spidroin
Biomacromolecules, 15:468-477, 2014

PubMed Abstract: C-terminal domains (CTDs) of various spidroins are relatively conserved in the amino acid sequence and have been suggested to perform similar functions. Here, we solved the structure of the CTD of an aciniform spidroin using NMR spectroscopy with a two-point mutant and studied its functional role with several constructs. The CTDs of aciniform, major, and minor ampullate spidroins adopt the same domain-swapping dimeric folding although their sequence identities are 24-40%. Unlike CTDs of major and minor ampullate spidroins, the aciniform CTD had no obvious effects on preventing spidroins from aggregation in storage but slightly enhanced protein assembly under shear force. The differential functions may result from significant differences in detailed structures and properties of repetitive regions of various types of spidroins. Nevertheless, all CTDs may have a common functional role: dimerization of the CTD doubles the size of silk proteins, reduces the number of chain ends, and thus leads to fewer chain end defects in the fibers formed.

PubMed: 24422432
DOI: 10.1021/bm401709v

Experimental method

SOLUTION NMR