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Record 11 of 865
Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
Author and Affiliation:
Lim, K.(NASA Marshall Space Flight Center, Huntsville, AL United States)
Ho, J. X.
Keeling, K.
Gilliland, G. L.
Ji, X.
Ruker, F.
Carter, D. C.
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.
Publication Date: Dec 01, 1994
Document ID:
20040188788
(Acquired Dec 14, 2004)
Subject Category: LIFE SCIENCES (GENERAL)
Document Type: Journal Article
Publication Information: Protein science : a publication of the Protein Society (ISSN 0961-8368); Volume 3; 12; 2233-44
Publisher Information: United States
Description: In English
Distribution Limits: Unclassified; Publicly available; Unlimited
Rights: Copyright
NASA Terms: AMINO ACIDS; ANTIGENS; ENZYMES; ENZYMOLOGY; GLUTATHIONE; HUMAN IMMUNODEFICIENCY VIRUS; IMMUNE SYSTEMS; PROTEINS; WORMS; ACTIVE SITES (CHEMISTRY); ANTIBODIES; CRYSTALLOGRAPHY; GENETICS; HOMOLOGY; MODELS; PHYSICAL CHEMISTRY; RATS; X RAY DIFFRACTION
Other Descriptors: EPITOPES/CHEMISTRY/GENETICS/IMMUNOLOGY; HIV ENVELOPE PROTEIN GP41/CHEMISTRY/GENETICS/IMMUNOLOGY; HIV-1/GENETICS/IMMUNOLOGY; HELMINTH PROTEINS/CHEMISTRY/GENETICS/IMMUNOLOGY; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS/CHEMISTRY/IMMUNOLOGY; SCHISTOSOMA JAPONICUM/ENZYMOLOGY/GENETICS/IMMUNOLOGY; AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL/IMMUNOLOGY; BINDING SITES; CHEMISTRY, PHYSICAL; COMPARATIVE STUDY; CRYSTALLOGRAPHY, X-RAY; GLUTATHIONE; GLUTATHIONE TRANSFERASE/METABOLISM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S
Availability Source: Other Sources
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