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

Ariadna B. Juárez-Martínez, Rogerio R. Sotelo-Mundo, Enrique Rudiño-Piñera

Resultado de la investigación: Contribución a una revistaArtículo

Resumen

Glutathione S-transferases (GSTs) are dimeric proteins that play a key role in phase II cellular detoxification. Here, the first crystal structure of a GST class-mu from marine crustacean shrimp Litopenaeus vannamei is reported at a resolution of 2.0 Å. The coordinates reported here have the lowest sequence identity with previously reported GSTs class-mu deposited at the Protein Data Bank (PDB), although they have subtle conformational differences. One key feature of GST class-mu from L. vannamei is the active site crevice markedly reduced when it is compared with other GSTs class-mu. This finding together with the chemical change of residues into the cavity (F112 and Y210) points to a particular specialization in which smallest xenobiotics with nonstandard chemical characteristics can be bound to the H-site. This suggests that marine organisms have evolved structural strategies to provide efficient selectivity toward xenobiotics to be disposed of by the phase II detoxification process.

Idioma originalInglés
Número de artículoe21838
PublicaciónJournal of Biochemical and Molecular Toxicology
Volumen31
N.º2
DOI
EstadoPublicada - 1 feb 2017

Huella dactilar

Xenobiotics
Glutathione Transferase
Crystal structure
Binding Sites
Phase II Metabolic Detoxication
Molecules
Detoxification
Aquatic Organisms
Catalytic Domain
Proteins
Databases

Citar esto

@article{8722e9f9310d4e788a1d6af103c3ccea,
title = "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",
abstract = "Glutathione S-transferases (GSTs) are dimeric proteins that play a key role in phase II cellular detoxification. Here, the first crystal structure of a GST class-mu from marine crustacean shrimp Litopenaeus vannamei is reported at a resolution of 2.0 {\AA}. The coordinates reported here have the lowest sequence identity with previously reported GSTs class-mu deposited at the Protein Data Bank (PDB), although they have subtle conformational differences. One key feature of GST class-mu from L. vannamei is the active site crevice markedly reduced when it is compared with other GSTs class-mu. This finding together with the chemical change of residues into the cavity (F112 and Y210) points to a particular specialization in which smallest xenobiotics with nonstandard chemical characteristics can be bound to the H-site. This suggests that marine organisms have evolved structural strategies to provide efficient selectivity toward xenobiotics to be disposed of by the phase II detoxification process.",
keywords = "Litopenaeus vannamei, class-mu GST, glutathione, glutathione S-transferase, whiteleg shrimp",
author = "Ju{\'a}rez-Mart{\'i}nez, {Ariadna B.} and Sotelo-Mundo, {Rogerio R.} and Enrique Rudi{\~n}o-Pi{\~n}era",
year = "2017",
month = "2",
day = "1",
doi = "10.1002/jbt.21838",
language = "Ingl{\'e}s",
volume = "31",
journal = "Journal of Biochemical and Molecular Toxicology",
issn = "1095-6670",
publisher = "John Wiley and Sons Inc.",
number = "2",

}

TY - JOUR

T1 - Crystal structure of a class-mu glutathione S-transferase from whiteleg shrimp Litopenaeus vannamei

T2 - structural changes in the xenobiotic binding H-site may alter the spectra of molecules bound

AU - Juárez-Martínez, Ariadna B.

AU - Sotelo-Mundo, Rogerio R.

AU - Rudiño-Piñera, Enrique

PY - 2017/2/1

Y1 - 2017/2/1

N2 - Glutathione S-transferases (GSTs) are dimeric proteins that play a key role in phase II cellular detoxification. Here, the first crystal structure of a GST class-mu from marine crustacean shrimp Litopenaeus vannamei is reported at a resolution of 2.0 Å. The coordinates reported here have the lowest sequence identity with previously reported GSTs class-mu deposited at the Protein Data Bank (PDB), although they have subtle conformational differences. One key feature of GST class-mu from L. vannamei is the active site crevice markedly reduced when it is compared with other GSTs class-mu. This finding together with the chemical change of residues into the cavity (F112 and Y210) points to a particular specialization in which smallest xenobiotics with nonstandard chemical characteristics can be bound to the H-site. This suggests that marine organisms have evolved structural strategies to provide efficient selectivity toward xenobiotics to be disposed of by the phase II detoxification process.

AB - Glutathione S-transferases (GSTs) are dimeric proteins that play a key role in phase II cellular detoxification. Here, the first crystal structure of a GST class-mu from marine crustacean shrimp Litopenaeus vannamei is reported at a resolution of 2.0 Å. The coordinates reported here have the lowest sequence identity with previously reported GSTs class-mu deposited at the Protein Data Bank (PDB), although they have subtle conformational differences. One key feature of GST class-mu from L. vannamei is the active site crevice markedly reduced when it is compared with other GSTs class-mu. This finding together with the chemical change of residues into the cavity (F112 and Y210) points to a particular specialization in which smallest xenobiotics with nonstandard chemical characteristics can be bound to the H-site. This suggests that marine organisms have evolved structural strategies to provide efficient selectivity toward xenobiotics to be disposed of by the phase II detoxification process.

KW - Litopenaeus vannamei

KW - class-mu GST

KW - glutathione

KW - glutathione S-transferase

KW - whiteleg shrimp

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U2 - 10.1002/jbt.21838

DO - 10.1002/jbt.21838

M3 - Artículo

C2 - 27717103

AN - SCOPUS:85013301806

VL - 31

JO - Journal of Biochemical and Molecular Toxicology

JF - Journal of Biochemical and Molecular Toxicology

SN - 1095-6670

IS - 2

M1 - e21838

ER -