4OFM

Triclinic NaGST1

Summary for 4OFM

• Entry DOI: 10.2210/pdb4ofm/pdb
• Related: 2ON7 4OFN 4OFT
• Descriptor: Glutathione S-transferase-1, GLUTATHIONE (3 entities in total)
• Functional Keywords: gst, transferase
• Biological source: Necator americanus (Human hookworm)
• Total number of polymer chains: 4
• Total formula weight: 96070.73

Authors

Asojo, O.A. (deposition date: 2014-01-15, release date: 2014-12-03, Last modification date: 2023-09-20)

Primary citation

Asojo, O.A.,Ceccarelli, C.
Structure of glutathione S-transferase 1 from the major human hookworm parasite Necator americanus (Na-GST-1) in complex with glutathione.
Acta Crystallogr F Struct Biol Commun, 70:1162-1166, 2014

PubMed 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.

PubMed: 25195885
DOI: 10.1107/S2053230X1401646X

Experimental method

X-RAY DIFFRACTION (2.64 Å)