Article
Multidisciplinary Sciences
Mathieu Botte, Dongchun Ni, Stephan Schenck, Iwan Zimmermann, Mohamed Chami, Nicolas Bocquet, Pascal Egloff, Denis Bucher, Matilde Trabuco, Robert K. Y. Cheng, Janine D. Brunner, Markus A. Seeger, Henning Stahlberg, Michael Hennig
Summary: Researchers report the structure of a partially opened LptDE transporter and its complex with rigid chaperones derived from nanobodies. The study provides insights into the mechanism of LPS insertion, offers a structural framework for the development of antibiotics targeting LptD, and describes a highly rigid chaperone scaffold for structural biology research on challenging protein targets.
NATURE COMMUNICATIONS
(2022)
Article
Chemistry, Physical
Jia-Liang Chen, Xiao Wang, Feng Yang, Bin Li, Gottfried Otting, Xun-Cheng Su
Summary: We report the solution structure of an authentic sortaseA thioester intermediate with the bound substrate. Through advanced techniques, we determined the 3D structure of this short-lived enzymatic reaction intermediate at atomic resolution. The formation and stability of the intermediate are influenced by calcium binding and its interaction with the substrate, highlighting the importance of calcium in the function of sortase A.
Article
Biochemistry & Molecular Biology
Midori Usami, Koki Ando, Asuka Shibuya, Ryoko Takasawa, Hideshi Yokoyama
Summary: Human glyoxalase I (hGLO I) is an enzyme that detoxifies methylglyoxal (MG) and is a promising target for anticancer drug development. The crystal structures of hGLO I and its complex with the GLO I inhibitor TLSC702 were determined, providing a structural basis for the development of improved anticancer drugs.
Article
Biochemistry & Molecular Biology
Apisan Phienluphon, Keiko Kondo, Bunzo Mikami, Takashi Nagata, Masato Katahira
Summary: This study investigates the molecular mechanisms of substrate recognition and catalysis by AsFaeE esterase through X-ray crystallography and kinetic analysis. The findings provide insights into the structure-function relationship of AsFaeE and identify distinct substrate-binding mechanisms compared to other FAEs.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Biochemistry & Molecular Biology
Chao Shi, Mingyue Gu, Zhangxin Chen, Xiaonan Huang, Juan Guo, Luqi Huang, Jie Deng, Ke He, Lei Zhang, Lixin Huang, Zhenzhan Chang
Summary: The study revealed the crystal structures of CYP76AH1 and its natural substrate miltiradiene, providing important insights into its catalytic mechanism and the basis for improving tanshinone production.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Microbiology
Yang Li, Zhen Rong, Zhengyang Li, Henglin Cui, Jixi Li, Xue-Wei Xu
Summary: In this study, a marine microbial carboxylesterase named E93 was found to hydrolyze both CPT11 and NPC substrates. Structural analysis revealed the interaction patterns between the enzyme and the substrates, and three core regions were identified to be involved in substrate specificity. These findings contribute to the understanding of substrate specificity and potential application of microbial Family VII carboxylesterases.
FRONTIERS IN MICROBIOLOGY
(2023)
Article
Multidisciplinary Sciences
Baohua Chen, Zheng Liu, Kay Perry, Rongsheng Jin
Summary: The study reveals the mechanism of how toxin A from Clostridioides difficile causes diarrhea by glucosylating and inactivating Rho and Ras family small GTPases, providing insights into substrate recognition.
SCIENTIFIC REPORTS
(2022)
Article
Chemistry, Multidisciplinary
Tiezheng Pan, Basudev Maity, Satoshi Abe, Taiki Morita, Takafumi Ueno
Summary: The emergence of protein-based crystalline materials provides promising opportunities for enzyme immobilization. This study demonstrates the use of polyhedra crystals to simultaneously encapsulate the foreign enzymes FDH and the organic photocatalyst eosin Y. These hybrid protein crystals, prepared easily by cocrystallization within a cell, form solid particles at a scale of 1 μm without the need for complex purification processes. The immobilized FDH within protein crystals exhibits recyclability, thermal stability, and maintains 94.4% activity compared to the free enzyme. Additionally, the incorporation of eosin Y enables CO(2)-formate conversion activity in the solid catalyst through a cascade reaction. This work highlights the potential of engineering protein crystals for the development of robust and environmentally friendly solid catalysts for artificial photosynthesis.
Article
Chemistry, Physical
Vania Brissos, Patricia T. Borges, Reyes Nunez-Franco, Maria Fatima Lucas, Carlos Frazao, Emanuele Monza, Laura Masgrau, Tiago N. Cordeiro, Ligia O. Martins
Summary: This study characterizes the molecular features of the evolution of a hyperthermostable metallo-oxidase from the multicopper oxidase family into a laccase by combining mutagenesis with structural, kinetic, and in silico analyses. The results show that residue replacements and distal mutations modulate substrate binding and catalysis, and allosterically coupled, long-range dynamic networks favor catalytically competent conformational states.
Article
Biochemistry & Molecular Biology
Hui Lin, Peng Xiao, Rui-Qian Bu, Shengchao Guo, Zhao Yang, Daopeng Yuan, Zhong-Liang Zhu, Chuan-Xin Zhang, Qing-Tao He, Chao Zhang, Yu-Qi Ping, Ru-Jia Zhao, Chuan-Shun Ma, Chang-Hao Liu, Xiao-Ning Zhang, Dan Jiang, Shaohui Huang, Yue-Tong Xi, Dao-Lai Zhang, Chen-Yang Xue, Bai-Sheng Yang, Jian-Yuan Li, Hao-Cheng Lin, Xu-Hui Zeng, Han Zhao, Wen-Ming Xu, Fan Yi, Zhongmin Liu, Jin-Peng Sun, Xiao Yu
Summary: In this study, the cryo-EM structure of apo-ADGRG2 in complex with a G(s) trimer was solved, providing insights into the activation and ligand-binding of ADGRG2. The identification of steroid hormones, such as DHEA, as potential ligands of ADGRG2 was also reported.
NATURE CHEMICAL BIOLOGY
(2022)
Article
Cell Biology
Melissa S. Traver, Sarah E. Bradford, Jose Luis Olmos, Zachary J. Wright, Mitchell D. Miller, Weijun Xu, George N. Phillips, Bonnie Bartel
Summary: This study reports the crystal structure of the PEX4-PEX22 peroxin complex from Arabidopsis thaliana. PEX4 is a ubiquitin-conjugating enzyme that ubiquitinates proteins associated with the peroxisomal membrane, while PEX22 anchors PEX4 and facilitates its activity. The structure of the Arabidopsis PEX4-PEX22 complex is similar to its yeast orthologs and reveals the potential role of a mutant residue in peroxisomal dysfunction.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2022)
Article
Mathematics, Applied
Quanxiang Pan
Summary: In this paper, we have shown that an almost contact metric structure of a real hypersurface in a complex space form is quasi-contact if and only if it is contact. We have also classified real hypersurfaces whose associated almost contact metric structures are nearly Kenmotsu or cosymplectic, which extends some earlier results in this field.
Article
Agriculture, Multidisciplinary
Tingting Ran, Linshu Jiao, Weiwu Wang, Juhua Chen, Huibing Chi, Zhaoxin Lu, Chong Zhang, Dongqing Xu, Fengxia Lu
Summary: The study identified two additional tyrosines in BlAsnase that are important for the binding and catalysis of D-asparagine. Substituting Tyr278 with methionine weakened the interaction with D-asparagine, leading to a loss of hydrolyzing function.
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
(2021)
Article
Biology
Ahmed-Noor A. Agip, Injae Chung, Alvaro Sanchez-Martinez, Alexander J. Whitworth, Judy Hirst
Summary: Respiratory complex I in Drosophila melanogaster has a 43-subunit structure with high homology to the mammalian counterpart. It is in a mammalian-type active resting state, with a fully ordered and enclosed ubiquinone-binding site, but with subtle conformational changes. The deactive resting state observed in mammals is not seen, but minor states with a deactive-type pi-bulge in subunit ND6-TMH3 are present.
Article
Chemistry, Physical
Sicong Li, Priscila dos Santos Bury, Fanglu Huang, Junhong Guo, Guo Sun, Anna Reva, Chuan Huang, Xinyun Jian, Yuan Li, Jiahai Zhou, Zixin Deng, Finian J. Leeper, Peter F. Leadlay, Marcio V. B. Dias, Yuhui Sun
Summary: The study reveals the dideoxygenation process of intermediates JI-20A and JI-20B in gentamicin, starting with phosphorylation catalyzed by GenP and then modified by GenB3 and GenB4 to form gentamicin C complex. Insights into the catalytic mechanisms of GenB3 and GenB4 are provided through crystal structures and site-directed mutagenesis.