7WWN

Structure of hypothetical protein TTHA1873 from Thermus thermophilus with Potassium mercuric iodide

Summary for 7WWN

• Entry DOI: 10.2210/pdb7wwn/pdb
• Descriptor: hypothetical protein TTHA1873, CALCIUM ION, tetraiodomercurate(2-), ... (4 entities in total)
• Functional Keywords: unknown function
• Biological source: Thermus thermophilus HB8
• Total number of polymer chains: 1
• Total formula weight: 22097.38

Authors

Yuvaraj, I.,Sekar, K. (deposition date: 2022-02-14, release date: 2022-04-06, Last modification date: 2024-05-29)

Primary citation

Yuvaraj, I.,Chaudhary, S.K.,Jeyakanthan, J.,Sekar, K.
Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.
Acta Crystallogr.,Sect.F, 78:338-346, 2022

PubMed 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: P422 and P622. 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 Ca 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.

PubMed: 36048084
DOI: 10.1107/S2053230X22008457

Experimental method

X-RAY DIFFRACTION (2.05 Å)