嗜热栖热菌 hypothetical 蛋白 TTHA1873 的结构。
Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.
机构信息
Department of Computational and Data Sciences, Indian Institute of Science, Bangalore 560 012, India.
Structural Biology and Bio Computing Laboratory, Department of Bioinformatics, Alagappa University, Karaikudi 630 004, India.
出版信息
Acta Crystallogr F Struct Biol Commun. 2022 Sep 1;78(Pt 9):338-346. doi: 10.1107/S2053230X22008457. Epub 2022 Aug 30.
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.
来自嗜热栖热菌的未鉴定假设蛋白 TTHA1873 的晶体结构已通过 X 射线晶体学确定，分辨率为 1.78Å，使用单波长异常分散法。该蛋白以两种空间群：P422 和 P622 的形式二聚体结晶。对假设蛋白的结构分析表明，TTHA1873 的整体折叠具有 β-三明治果冻卷拓扑结构，有九个 β-链。TTHA1873 是一种二聚体金属结合蛋白，每个链结合两个 Ca 离子，一个在表面，另一个稳定两个链的二聚体界面。结构同源性搜索表明，该蛋白与细胞表面蛋白或凝集素受体蛋白的一个结构域具有中等结构相似性。在高浓度的假设蛋白存在下，红细胞表现出明显的聚集。
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