5Z1Q

Crystal structures of the trimeric N-terminal domain of Ciliate Euplotes octocarinatus Centrin

Summary for 5Z1Q

• Entry DOI: 10.2210/pdb5z1q/pdb
• Descriptor: Centrin protein, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: certrin, trimer, calcium ion, ciliate euplotes octocarinatus, metal binding protein
• Biological source: Euplotes octocarinatus
• Total number of polymer chains: 3
• Total formula weight: 34631.31

Authors

Wang, W.,Zhao, Y.,Yang, B.,Wang, H. (deposition date: 2017-12-27, release date: 2018-04-25, Last modification date: 2024-11-20)

Primary citation

Wang, W.,Zhao, Y.,Wang, H.,Yang, B.
Crystal structure of the trimeric N-terminal domain of ciliate Euplotes octocarinatus centrin binding with calcium ions
Protein Sci., 27:1102-1108, 2018

PubMed Abstract: Centrin is a member of the EF-hand superfamily of calcium-binding proteins, a highly conserved eukaryotic protein that binds to Ca . Its self-assembly plays a causative role in the fiber contraction that is associated with the cell division cycle and ciliogenesis. In this study, the crystal structure of N-terminal domain of ciliate Euplotes octocarinatus centrin (N-EoCen) was determined by using the selenomethionine single-wavelength anomalous dispersion method. The protein molecules formed homotrimers. Every protomer had two putative Ca ion-binding sites I and II, protomer A, and C bound one Ca ion, while protomer B bound two Ca ions. A novel binding site III was observed and the Ca ion was located at the center of the homotrimer. Several hydrogen bonds, electrostatic, and hydrophobic interactions between the protomers contributed to the formation of the oligomer. Structural studies provided insight into the foundation for centrin aggregation and the roles of calcium ions.

PubMed: 29607555
DOI: 10.1002/pro.3418

Experimental method

X-RAY DIFFRACTION (2.3 Å)