Structure of glutathione S‐transferase 1 from the major human hookworm parasite Necator americanus (Na‐GST‐1) in complex with glutathione. Issue 9 (1st September 2014)

• Record Type: Journal Article
• Authors: Asojo, Oluwatoyin A.; Ceccarelli, Christopher
• Is Part Of: Acta crystallographica. Volume 70:Issue 9(2014:Sep.)
• Page Start: 1162
• Page End: 1166
• Publication Date: 2014-09-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1401646X
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Glutathione <italic>S</italic>‐transferase 1 from <italic>Necator americanus</italic> (<italic>Na</italic>‐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 <italic>Na</italic>‐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 <italic>Na</italic>‐GST‐1 with any of these molecules, co‐crystallization experiments resulted in the first structures of the complex of <italic>Na</italic>‐GST‐1 with the substrate glutathione. The structures of the complex of <italic>Na</italic>‐GST‐1 with glutathione were solved from pathological crystalline aggregates comprising more than one crystal form. These first structures of the complex of <italic>Na</italic>‐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.</p> </abstract>