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Solution NMR

Solution Structure of putative anti sigma factor antagonist from Thermotoga maritima (TM1442)

Released:
DOI: 10.2210/pdb1sbo/pdb
PDB entry 1sbo coloured by chain, ensemble of 20 models, front view.
PDB entry 1sbo coloured by chain, ensemble of 20 models, side view.
PDB entry 1sbo coloured by chain, ensemble of 20 models, top view.
Source organism: Thermotoga maritima
Primary publication:
Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.
Etezady-Esfarjani T, Placzek WJ, Herrmann T, Wüthrich K
Magn Reson Chem 44 Spec No S61-70 (2006)
PMID: 16826544

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative anti-sigma factor antagonist TM_1442 Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.32 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9X1F5 (Residues: 1-110; Coverage: 100%)
Gene name: TM_1442
Sequence domains: STAS domain
Structure domains: STAS domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli BL21

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Citations

5 citation in other articles

Automated amino acid side-chain NMR assignment of proteins using (13)C- and (15)N-resolved 3D [ (1)H, (1)H]-NOESY.
Fiorito et al. (2008)
4 more

8 mentions without citation

Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.
Shammas et al. (2016)
7 more