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 P6...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2022-09, Vol.78 (9), p.338-346
Main Authors: Yuvaraj, I., Chaudhary, Santosh Kumar, Jeyakanthan, J., Sekar, K.
Format: Article
Language:English
Subjects:
Agglutination
Calcium ions
calcium‐binding proteins
Cell surface
Chains
Crystal structure
Crystallization
Crystallography
Dimers
Erythrocytes
Homology
hypothetical proteins
jelly‐roll topology
metalloproteins
Protein folding
Protein structure
Proteins
Research Communications
SAD phasing
Structural analysis
Thermus thermophilus
Topology
TTHA1873
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Summary: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. The crystal structure of the hypothetical protein TTHA1873 from T. thermophilus has been determined using X‐ray crystallography. At high concentrations, the protein showed visible agglutination of red blood cells; its structural properties and thermal stability are discussed.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X22008457