Crystal structure of TTHA0061, an uncharacterized protein from Thermus thermophilus HB8, reveals a novel fold

The crystal structure of an uncharacterized protein TTHA0061 from Thermus thermophilus HB8, was determined and refined to 1.8 Å by a single wavelength anomalous dispersion (SAD) method. The structural analysis and comparison of TTHA0061 with other existing structures in the Protein Data Bank (PDB) revealed a novel fold, suggesting that this protein may belong to a translation initiation factor or ribosomal protein family. Differential scanning calorimetry analysis suggested that the thermostability of TTHA0061 increased at pH ranges of 5.8–6.2, perhaps due to the abundance of glutamic acid residues.

Research highlights
► Crystal structure of an uncharacterized protein TTHA0061 from Thermusthermophilus HB8, was determined.
► The overall structure of TTHA0061 revealed a novel fold.
► Structural analyses suggested that it may belong to a translation initiation factor or ribosomal protein family.
► The increment of thermo stability of the TTHA0061 at different pHs were analyzed by DSC and discussed.