PDBsum entry 4ofm

Transferase

PDB id: 4ofm

Contents

Protein chains

205 a.a.

Ligands

GSH ×4

Waters ×99

PDB id:

4ofm

Name:

Transferase

Title:

Triclinic nagst1

Structure:

Glutathione s-transferase-1. Chain: a, b, c, d. Engineered: yes

Source:

Necator americanus. Human hookworm. Organism_taxid: 51031. Gene: gst-1. Expressed in: komagataella pastoris. Expression_system_taxid: 4922.

Resolution:

2.64Å R-factor: 0.222 R-free: 0.269

Authors:

O.A.Asojo

Key ref:

O.A.Asojo and C.Ceccarelli (2014). 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. PubMed id: 25195885 DOI: 10.1107/S2053230X1401646X

Date:

15-Jan-14 Release date: 03-Dec-14

Protein chains

D3U1A5  (D3U1A5_NECAM) -  glutathione transferase from Necator americanus

Seq: 206 a.a.

Struc: 205 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1107/S2053230X1401646X

Acta Crystallogr F Struct Biol Commun 70:1162-1166 (2014)

PubMed id: 25195885

Structure of glutathione S-transferase 1 from the major human hookworm parasite Necator americanus (Na-GST-1) in complex with glutathione.

O.A.Asojo, C.Ceccarelli.

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.