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Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.

ABSTRACT: 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.

SUBMITTER: Yuvaraj I

PROVIDER: S-EPMC9435673 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.

Yuvaraj I I Chaudhary Santosh Kumar SK Jeyakanthan J J Sekar K K

Acta crystallographica. Section F, Structural biology communications 20220830 Pt 9

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 ...[more]

PMID: 36048084

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