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150 results on '"Ran, Tingting"'

10. Structural insight into subunit F of respiratory chain complex I from Xanthomonas oryzae pv. oryzae inhibition by parthenolide.

Author

Li, Lei, Zhou, Qian, Li, Linwei, Ran, Tingting, Wang, Weiwu, Liu, Chenyang, Chen, Jin, Sun, Tiemin, Chen, Yu, Feng, Xu, Zhang, Feng, and Xu, Shu

Subjects
XANTHOMONAS oryzae, RICE diseases & pests, BINDING sites, PROTEIN structure, MOLECULAR docking, XANTHOMONAS, BACTERICIDES
Abstract

BACKGROUND: Bacterial leaf blight caused by Xanthomonas oryzae pv. oryzae (Xoo) is one of the most serious diseases of rice, and there is a lack of bactericides for controlling this disease. We previously found parthenolide (PTL) is a potential lead for developing bactericides against Xoo, and subunit F of respiratory chain complex I (NuoF) is an important target protein of PTL. However, the binding modes of PTL with NuoF need further elucidation. RESULTS: In this study, we obtained the crystal structure of Xoo NuoEF (complex of subunit E and F of respiratory chain complex I) with a resolution of 2.36 Å, which is the first report on the protein structure of NuoEF in plant‐pathogenic bacteria. The possible binding sites of PTL with NuoF (Cys105 and Cys187) were predicted with molecular docking and mutated into alanine using a base mismatch method. The mutated proteins were expressed in Escherichia coli and purified with affinity chromatography. The binding abilities of PTL with mutated proteins were investigated via pull‐down assay and BIAcore analysis, which revealed that double mutation of Cys105 and Cys187 in NuoF severely affected the binding ability of PTL with NuoF. In addition, the binding modes were further simulated with combined quantum mechanical/molecular mechanical calculations, and the results indicated that PTL may have a stronger binding with Cys105 than Cys187. CONCLUSION: NuoEF protein structure of Xoo was resolved, and Cys105 and Cys187 in NuoF are important binding sites of PTL. This study further clarified the action mechanism of PTL against Xoo, and will promote the innovation of bactericides targeting Xoo complex I. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Published
2024
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21. Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases

Author

Chen, Rong, primary, Zhao, Lin, additional, Gan, Rong, additional, Feng, Zhixin, additional, Cui, Chenxi, additional, Xie, Xing, additional, Hao, Fei, additional, Zhang, Zhenzhen, additional, Wang, Li, additional, Ran, Tingting, additional, Wang, Weiwu, additional, Zhang, Shuijun, additional, Li, Yufeng, additional, Zhang, Wei, additional, Pang, Maoda, additional, Xiong, Qiyan, additional, and Shao, Guoqing, additional

Published
2022
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33. Structures of l-asparaginase from Bacillus licheniformisReveal an Essential Residue for its Substrate Stereoselectivity

Author

Ran, Tingting, Jiao, Linshu, Wang, Weiwu, Chen, Juhua, Chi, Huibing, Lu, Zhaoxin, Zhang, Chong, Xu, Dongqing, and Lu, Fengxia

Abstract

l-Asparaginase, which catalyzes the hydrolysis of l-asparagine, is an important enzyme in both the clinical and food industry. Exploration of efficient l-asparaginase with high substrate specificity, especially high chiral selectivity, is essential for extending its use. Herein, various crystal structures of type I l-asparaginase from Bacillus licheniformis(BlAsnase) have been resolved, and we found that there are two additional tyrosines in BlAsnase, contributing to the binding and catalysis of d-asparagine. Strikingly, the substitution of Tyr278 with methionine impaired the interaction with d-asparagine via water molecules due to the small hydrophobic side chain of methionine, which forced the ligand to the deep side of the active site toward the catalytic residues and thus resulted in the loss of hydrolyzing function. Our investigation of the substrate recognition mechanism of BlAsnase is significant for both a better understanding of l-asparaginase and its rational design to achieve high specificity for clinical and industrial applications.

Published
2021
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41. Differential roles for ArcA and ArcB homologues in swarming motility in <italic>Serratia marcescens</italic> FS14.

Author

Zhang, Xiaolan, Wu, Defeng, Guo, Tengfei, Ran, Tingting, Wang, Weiwu, and Xu, Dongqing

Abstract

ArcAB is a two-component regulatory system that can help bacteria respond to and survive in a changing environment. To identify the function of ArcAB homologues in Serratia marcescens FS14, in-frame deletion mutants of the arcA, arcB and arcAB genes were constructed. Surprisingly, ArcB affects the motility of FS14, but ArcA does not. These results are the reverse of those found in Escherichia coli. Further studies demonstrated that ArcB could promote bacterial motility by activating the synthesis of flagella and particularly by activating the expression of the biosurfactant serrawettin W1. Our results suggest that ArcB may regulate FS14 motility by interacting with an unidentified response regulator other than ArcA. The regulation of ArcAB may be bacterial strain-specific, and the same regulatory system may participate in different mechanisms to adapt to different environments. [ABSTRACT FROM AUTHOR]

Published
2018
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