The interaction between lanthanide (III) and N-terminal domain of Euplotes octocarinatus centrin

2012 ◽  
Vol 87 ◽  
pp. 163-170 ◽  
Author(s):  
Yaqin Zhao ◽  
Jun Yan ◽  
Li Song ◽  
Yanan Feng ◽  
Aihua Liang ◽  
...  
Keyword(s):  
Terminal Domain ◽  
Euplotes Octocarinatus

scholarly journals Crystal structure of the trimeric N-terminal domain of ciliate Euplotes octocarinatus centrin binding with calcium ions

2018 ◽  
Vol 27 (6) ◽  
pp. 1102-1108 ◽  
Author(s):  
Wenming Wang ◽  
Yaqin Zhao ◽  
Hongfei Wang ◽  
Bingsheng Yang
Keyword(s):  
Crystal Structure ◽  
Calcium Ions ◽  
Terminal Domain ◽  
Euplotes Octocarinatus

scholarly journals Endonuclease-like activity of the N-terminal domain of Euplotes octocarinatus centrin

RSC Advances ◽  
2017 ◽  
Vol 7 (82) ◽  
pp. 51773-51788 ◽  
Author(s):  
Wenlong Zhang ◽  
Enxian Shi ◽  
Yanan Feng ◽  
Yaqin Zhao ◽  
Binsheng Yang
Keyword(s):  
Nucleotide Excision Repair ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Excision Repair ◽  
Calcium Binding Proteins ◽  
Terminal Domain ◽  
Nucleotide Excision ◽  
Ef Hand ◽  
Euplotes Octocarinatus

Euplotes octocarinatus centrin (EoCen) is a member of the EF-hand superfamily of calcium-binding proteins, which refer to nucleotide excision repair (NER).

Analysis of Tb3+- and melittin-binding with the C-terminal domain of centrin in Euplotes octocarinatus

2012 ◽  
Vol 132 (4) ◽  
pp. 924-930 ◽  
Author(s):  
Ya-Qin Zhao ◽  
Xiu-Ling Diao ◽  
Jun Yan ◽  
Ya-Nan Feng ◽  
Zhi-Jun Wang ◽  
...  
Keyword(s):  
Terminal Domain ◽  
Euplotes Octocarinatus

The acidic ribosomal protein P2 from Euplotes octocarinatus is phosphorylated at its N-terminal domain

2014 ◽  
Vol 92 (1) ◽  
pp. 23-32
Author(s):  
Miaoqing Hu ◽  
Luqin Li ◽  
Jianbing Chao ◽  
Yaqin Zhao ◽  
Zhiyun Zhang ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Phosphorylation Site ◽  
Elongation Factor ◽  
Native Page ◽  
Terminal Domain ◽  
Elongation Factor 2 ◽  
P Proteins ◽  
Euplotes Octocarinatus ◽  
Ribosomal P

The eukaryotic acid ribosomal P0, P1, and P2 proteins share a conserved flexible C-terminal tail that is rich in acidic residues, which are involved in the interaction with elongation factor 2 during protein synthesis. Our previous work suggested that the acidic ribosomal P proteins from Euplotes octocarinatus have a special C-terminal domain. To further understand this characteristic feature, both P2 and elongation factor 2 from E. octocarinatus were overexpressed, for the first time, in Escherichia coli in this study. GST pull-down assay indicated that P2 protein from E. octocarinatus (EoP2) interacted specifically with the N-terminal domain of elongation factor 2 from E. octocarinatus (EoEF-2) in vitro. The interacting part of EoP2 is in the C-terminal domains, consistent with the observation in other organisms. Phosphorylation of the recombinant EoP2 was performed in vitro using multiple methods such as 31P-NMR spectroscopy, native PAGE, and Phos-tagTM SDS-PAGE. Results showed that ribosomal protein EoP2 was phosphorylated by casein kinase II at serine 21 located at the N terminus. This phosphorylation site identified in EoP2 is quite different from that of P2 from other organisms, in which the phosphorylation site is located in the conserved C-terminal region.

Modulation of XPC peptide on binding Tb3+ to Euplotes octocarinatus centrin

Metallomics ◽  
2017 ◽  
Vol 9 (12) ◽  
pp. 1796-1808 ◽  
Author(s):  
Enxian Shi ◽  
Wenlong Zhang ◽  
Yaqin Zhao ◽  
Binsheng Yang
Keyword(s):  
Metal Ions ◽  
Peptide Binding ◽  
Terminal Domain ◽  
Euplotes Octocarinatus

Metal ions weakly enhanced the affinity between EoCen and the XPC peptide, whereas the peptide remarkably modulated the binding of Tb3+ to the N-terminal domain of EoCen. Peptide binding resulted in the dissociation of EoCen aggregates, and the aggregation of EoCen induced by Tb3+ binding was inhibited.

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1

2019 ◽  
Vol 476 (21) ◽  
pp. 3227-3240 ◽  
Author(s):  
Shanshan Wang ◽  
Yanxiang Zhao ◽  
Long Yi ◽  
Minghe Shen ◽  
Chao Wang ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Changes ◽  
Magnaporthe Oryzae ◽  
Structural Information ◽  
Complex Structure ◽  
Critical Role ◽  
Catalytic Process ◽  
Structural Basis ◽  
Salt Bridges ◽  
Terminal Domain

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (β3–β4 loop to α0 helix) and movement of a ‘shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a ‘closed' state compared with its ‘open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.

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