1GNE

THE THREE-DIMENSIONAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE OF SCHISTOSOMA JAPONICUM FUSED WITH A CONSERVED NEUTRALIZING EPITOPE ON GP41 OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1

Summary for 1GNE

• Entry DOI: 10.2210/pdb1gne/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, GLUTATHIONE (3 entities in total)
• Functional Keywords: glutathione transferase, transferase
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 27398.77

Authors

Lim, K.,Ho, J.X.,Keeling, K.,Gilliland, G.L.,Ji, X.,Ruker, F.,Carter, D.C. (deposition date: 1994-06-16, release date: 1994-11-30, Last modification date: 2023-08-30)

Primary citation

Lim, K.,Ho, J.X.,Keeling, K.,Gilliland, G.L.,Ji, X.,Ruker, F.,Carter, D.C.
Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV.
Protein Sci., 3:2233-2244, 1994

PubMed Abstract: The 3-dimensional crystal structure of glutathione S-transferase (GST) of Schistosoma japonicum (Sj) fused with a conserved neutralizing epitope on gp41 (glycoprotein, 41 kDa) of human immunodeficiency virus type 1 (HIV-1) (Muster T et al., 1993, J Virol 67:6642-6647) was determined at 2.5 A resolution. The structure of the 3-3 isozyme rat GST of the mu gene class (Ji X, Zhang P, Armstrong RN, Gilliland GL, 1992, Biochemistry 31:10169-10184) was used as a molecular replacement model. The structure consists of a 4-stranded beta-sheet and 3 alpha-helices in domain 1 and 5 alpha-helices in domain 2. The space group of the Sj GST crystal is P4(3)2(1)2, with unit cell dimensions of a = b = 94.7 A, and c = 58.1 A. The crystal has 1 GST monomer per asymmetric unit, and 2 monomers that form an active dimer are related by crystallographic 2-fold symmetry. In the binding site, the ordered structure of reduced glutathione is observed. The gp41 peptide (Glu-Leu-Asp-Lys-Trp-Ala) fused to the C-terminus of Sj GST forms a loop stabilized by symmetry-related GSTs. The Sj GST structure is compared with previously determined GST structures of mammalian gene classes mu, alpha, and pi. Conserved amino acid residues among the 4 GSTs that are important for hydrophobic and hydrophilic interactions for dimer association and glutathione binding are discussed.

PubMed: 7538846

Experimental method

X-RAY DIFFRACTION (2.5 Å)