Crystal structure of a class‐mu glutathione S‐transferase from whiteleg shrimp <i>Litopenaeus vannamei</i>: structural changes in the xenobiotic binding H‐site may alter the spectra of molecules bound

Juarez-Martinez, Ariadna B.; Sotelo‐Mundo, Rogerio R.; Rudino‐Pinera, E.

doi:10.1002/jbt.21838

Cited by 4 publications

(3 citation statements)

References 27 publications

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“…(F) GSH bound to LvGSTMu (PDB id 5an1) [38]. The interface comparisons of CdGSTM1-1 with different mu class GSTs showed similarities (Supplementary Table S1).…”

Section: Structure Comparison With Human Gstm1-1 and Other Gstmsmentioning

confidence: 99%

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Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1

Perperopoulou

Poudel

Papageorgiou

et al. 2022

Life

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Glutathione transferases (GSTs; EC. 2.5.1.18) are a large family of multifunctional enzymes that play crucial roles in the metabolism and inactivation of a broad range of xenobiotic compounds. In the present work, we report the kinetic and structural characterization of the isoenzyme GSTM1-1 from Camelus dromedarius (CdGSTM1-1). The CdGSΤM1-1 was expressed in E. coli BL21 (DE3) and was purified by affinity chromatography. Kinetics analysis showed that the enzyme displays a relative narrow substrate specificity and restricted ability to bind xenobiotic compounds. The crystal structures of CdGSΤM1-1 were determined by X-ray crystallography in complex with the substrate (GSH) or the reaction product (S-p-nitrobenzyl-GSH), providing snapshots of the induced-fit catalytic mechanism. The thermodynamic stability of CdGSTM1-1 was investigated using differential scanning fluorimetry (DSF) in the absence and in presence of GSH and S-p-nitrobenzyl-GSH and revealed that the enzyme’s structure is significantly stabilized by its ligands. The results of the present study advance the understanding of camelid GST detoxification mechanisms and their contribution to abiotic stress adaptation in harsh desert conditions.

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“…(F) GSH bound to LvGSTMu (PDB id 5an1) [38]. The interface comparisons of CdGSTM1-1 with different mu class GSTs showed similarities (Supplementary Table S1).…”

Section: Structure Comparison With Human Gstm1-1 and Other Gstmsmentioning

confidence: 99%

“…(E) GTX bound to CgGSTM1-1 (pdb ID 1gsu)[37]. (F) GSH bound to LvGSTMu (PDB id 5an1)[38]. Figure created with BIOVIA Discovery Studio.…”

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confidence: 99%

Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1

Perperopoulou

Poudel

Papageorgiou

et al. 2022

Life

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“…Here, we present the combination of templates that gave CpGST1, CpGST2 and CmGST3 models. The templates used to model CpGST1 were a Bombyx mori Sigma class GST (3VPQ-A) 85 that had 94% coverage and 26% identity and a Penaeus vannamei Mu class (5AN1-A) 86 with 98% coverage and 23% identity ( Fig. 3 and Table S5).…”

Section: Cryptosporidium Species Gsts Belongs To New Classes Phylogementioning

confidence: 99%

Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species

Mfeka

Martínez‐Oyanedel

Chen

et al. 2020

Sci Rep

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Cryptosporidiosis, caused by protozoan parasites of the genus Cryptosporidium, is estimated to rank as a leading cause in the global burden of neglected zoonotic parasitic diseases. This diarrheal disease is the second leading cause of death in children under 5 years of age. Based on the C. parvum transcriptome data, glutathione transferase (GST) has been suggested as a drug target against this pathogen. GSTs are diverse multifunctional proteins involved in cellular defense and detoxification in organisms and help pathogens to alleviate chemical and environmental stress. In this study, we performed genome-wide data mining, identification, classification and in silico structural analysis of GSTs in fifteen Cryptosporidium species. The study revealed the presence three GSTs in each of the Cryptosporidium species analyzed in the study. Based on the percentage identity and comprehensive comparative phylogenetic analysis, we assigned Cryptosporidium species GSTs to three new GST classes, named Vega (ϑ), Gamma (γ) and Psi (ψ). The study also revealed an atypical thioredoxin-like fold in the C. parvum GST1 of the Vega class, whereas C. parvum GST2 of the Gamma class and C. melagridis GST3 of the Psi class has a typical thioredoxin-like fold in the N-terminal region. This study reports the first comparative analysis of GSTs in Cryptosporidium species.

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Chemoprotection mediated by açaí berry (Euterpe oleracea) in white shrimp Litopenaeus vannamei exposed to the cyanotoxin saxitoxin analyzed by in vivo assays and docking modeling

et al. 2022

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Crystal structure of a class‐mu glutathione S‐transferase from whiteleg shrimp Litopenaeus vannamei: structural changes in the xenobiotic binding H‐site may alter the spectra of molecules bound

Cited by 4 publications

References 27 publications

Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1

Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1

Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species

Chemoprotection mediated by açaí berry (Euterpe oleracea) in white shrimp Litopenaeus vannamei exposed to the cyanotoxin saxitoxin analyzed by in vivo assays and docking modeling

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