1gne
From Proteopedia
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- | [[Image:1gne.jpg|left|200px]] | ||
- | + | ==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== | |
- | + | <StructureSection load='1gne' size='340' side='right'caption='[[1gne]], [[Resolution|resolution]] 2.50Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1gne]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GNE FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gne OCA], [https://pdbe.org/1gne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gne RCSB], [https://www.ebi.ac.uk/pdbsum/1gne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gne ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gn/1gne_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gne ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV.,Lim K, Ho JX, Keeling K, Gilliland GL, Ji X, Ruker F, Carter DC Protein Sci. 1994 Dec;3(12):2233-44. PMID:7538846<ref>PMID:7538846</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
+ | <div class="pdbe-citations 1gne" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | |
- | + | == References == | |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
- | [[Category: Carter | + | [[Category: Carter DC]] |
- | [[Category: Gilliland | + | [[Category: Gilliland GL]] |
- | [[Category: Ho | + | [[Category: Ho JX]] |
- | [[Category: Ji | + | [[Category: Ji X]] |
- | [[Category: Keeling | + | [[Category: Keeling K]] |
- | [[Category: Lim | + | [[Category: Lim K]] |
- | [[Category: Ruker | + | [[Category: Ruker F]] |
- | + | ||
- | + |
Current revision
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
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Categories: Large Structures | Synthetic construct | Carter DC | Gilliland GL | Ho JX | Ji X | Keeling K | Lim K | Ruker F