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Structure of glutathione S-transferase 1 from the major human hookworm parasite Necator americanus (Na-GST-1) in complex with glutathione.
Asojo, Oluwatoyin A; Ceccarelli, Christopher.
Afiliação
  • Asojo OA; National School of Tropical Medicine, Baylor College of Medicine, Houston, TX 77030, USA.
  • Ceccarelli C; National School of Tropical Medicine, Baylor College of Medicine, Houston, TX 77030, USA.
Acta Crystallogr F Struct Biol Commun ; 70(Pt 9): 1162-6, 2014 Sep.
Article em En | MEDLINE | ID: mdl-25195885
ABSTRACT
Glutathione S-transferase 1 from Necator americanus (Na-GST-1) is a vaccine candidate for hookworm infection that has a high affinity for heme and metal porphyrins. As part of attempts to clarify the mechanism of heme detoxification by hookworm GSTs, co-crystallization and soaking studies of Na-GST-1 with the heme-like molecules protoporphyrin IX disodium salt, hematin and zinc protoporphyrin were undertaken. While these studies did not yield the structure of the complex of Na-GST-1 with any of these molecules, co-crystallization experiments resulted in the first structures of the complex of Na-GST-1 with the substrate glutathione. The structures of the complex of Na-GST-1 with glutathione were solved from pathological crystalline aggregates comprising more than one crystal form. These first structures of the complex of Na-GST-1 with the substrate glutathione were solved by molecular replacement from data collected with a sealed-tube home source using the previously reported apo structure as the search model.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Necator americanus / Glutationa / Glutationa Transferase Limite: Animals Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Necator americanus / Glutationa / Glutationa Transferase Limite: Animals Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Estados Unidos