› 2m0m

Solution NMR

Structural Characterization of Minor Ampullate Spidroin Domains and their Distinct Roles in Fibroin Solubility and Fiber Formation

Released:
DOI: 10.2210/pdb2m0m/pdb
PDB entry 2m0m coloured by chain, ensemble of 10 models, front view.
PDB entry 2m0m coloured by chain, ensemble of 10 models, side view.
PDB entry 2m0m coloured by chain, ensemble of 10 models, top view.
Source organism: Trichonephila antipodiana
Primary publication:
Structural characterization of minor ampullate spidroin domains and their distinct roles in fibroin solubility and fiber formation.
Gao Z, Lin Z, Huang W, Lai CC, Fan JS, Yang D
PLoS One 8 e56142 (2013)
PMID: 23418525

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Minor ampullate fibroin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 107 amino acids
Theoretical weight: 10.51 KDa
Source organism: Trichonephila antipodiana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2LC34 (Residues: 250-356; Coverage: 30%)
Sequence domains: Major ampullate spidroin 1 and 2
Structure domains: Spidroin domain, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 41%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Toward spinning artificial spider silk.
Rising et al. (2015)
2 more

1 mention without citation

Carbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domains.
Andersson et al. (2014)