Backbone 1H, 15N, and 13C resonance assignments and secondary structure of a novel protein OGL-20P(T)-358 from hyperthermophile Thermococcus thioreducens sp. nov.
OGL-20P(T)-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain OGL-20PT, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone 1H, 15N, and 13C resonance assignments of OGL-20PT-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily alpha-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.
Wilson
Randall
R
Laboratory for Structural Biology, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
Hughes
Ronny
R
Curto
Ernest
E
Ng
Joseph
J
Twigg
Pamela
P
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D019712:Thermococcus / Q000737:chemistry*
D019843:Archaeal Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen