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6TV5

NMR structure of N-terminal domain from A. argentata tubuliform spidroin (TuSp) at pH 5.5

Summary for 6TV5
Entry DOI10.2210/pdb6tv5/pdb
NMR InformationBMRB: 34473
DescriptorTubuliform spidroin 1 (1 entity in total)
Functional Keywordsspidroin, n-terminal domain, spidersilk, structural protein
Biological sourceArgiope argentata
Total number of polymer chains2
Total formula weight28110.89
Authors
Fridmanis, J.,Jaudzems, K. (deposition date: 2020-01-09, release date: 2021-01-27, Last modification date: 2023-06-14)
Primary citationSede, M.,Fridmanis, J.,Otikovs, M.,Johansson, J.,Rising, A.,Kronqvist, N.,Jaudzems, K.
Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.
Front Mol Biosci, 9:936887-936887, 2022
Cited by
PubMed Abstract: The spidroin N-terminal domain (NT) is responsible for high solubility and pH-dependent assembly of spider silk proteins during storage and fiber formation, respectively. It forms a monomeric five-helix bundle at neutral pH and dimerizes at lowered pH, thereby firmly interconnecting the spidroins. Mechanistic studies with the NTs from major ampullate, minor ampullate, and flagelliform spidroins (MaSp, MiSp, and FlSp) have shown that the pH dependency is conserved between different silk types, although the residues that mediate this process can differ. Here we study the tubuliform spidroin (TuSp) NT from , which lacks several well conserved residues involved in the dimerization of other NTs. We solve its structure at low pH revealing an antiparallel dimer of two five-α-helix bundles, which contrasts with a previously determined TuSp NT monomer structure. Further, we study a set of mutants and find that the residues participating in the protonation events during dimerization are different from MaSp and MiSp NT. Charge reversal of one of these residues (R117 in TuSp) results in significantly altered electrostatic interactions between monomer subunits. Altogether, the structure and mutant studies suggest that TuSp NT monomers assemble by elimination of intramolecular repulsive charge interactions, which could lead to slight tilting of α-helices.
PubMed: 35775078
DOI: 10.3389/fmolb.2022.936887
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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