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- Title
Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.
- Authors
Yuvaraj, I.; Chaudhary, Santosh Kumar; Jeyakanthan, J.; Sekar, K.
- 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.
- Subjects
THERMUS thermophilus; PROTEIN structure; ERYTHROCYTES; X-ray crystallography; SPACE groups
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2022, Vol 78, Issue 9, p338
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X22008457