Structure of the hypothetical protein TTHA1873 from Thermus thermophilus

The crystal structure of an uncharacterized hypothetical protein, TTHA1873 from Thermus thermophilus, has been determined by X-ray crystallography to a resolution of 1.78   Å using the single-wavelength anomalous dispersion method. The protein crystallized as a dimer in two space groups: P43212 and P6122. Structural analysis of the hypothetical protein revealed that the overall fold of TTHA1873 has a β -sandwich jelly-roll topology with nine β -strands. TTHA1873 is a dimeric metal-binding protein that binds to two Ca2+ ions per chain, with one on the surface and the other stabilizing the dimeric interface of the two chains. A structural homology search indicates that the protein has moderate structural similarity to one domain of cell-surface proteins or agglutinin receptor proteins. Red blood cells showed visible agglutination at high concentrations of the hypothetical protein.

Source: Acta Crystallographica Section F - August 30, 2022 Category: Biochemistry Authors: Yuvaraj, I. Chaudhary, S.K. Jeyakanthan, J. Sekar, K. Tags: SAD phasing hypothetical proteins metalloproteins jelly-roll topology Thermus thermophilus TTHA1873 calcium-binding proteins research communications Source Type: research