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Publication Abstract from PubMed

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 A 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 beta-sandwich jelly-roll topology with nine beta-strands. TTHA1873 is a dimeric metal-binding protein that binds to two Ca(2+) 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.

Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.,Yuvaraj I, Chaudhary SK, Jeyakanthan J, Sekar K Acta Crystallogr F Struct Biol Commun. 2022 Sep 1;78(Pt 9):338-346. doi:, 10.1107/S2053230X22008457. Epub 2022 Aug 30. PMID:36048084^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.