1fhe: Difference between revisions

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[[Image:1fhe.gif|left|200px]]


<!--
==GLUTATHIONE TRANSFERASE (FH47) FROM FASCIOLA HEPATICA==
The line below this paragraph, containing "STRUCTURE_1fhe", creates the "Structure Box" on the page.
<StructureSection load='1fhe' size='340' side='right'caption='[[1fhe]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1fhe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fasciola_hepatica Fasciola hepatica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHE FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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>
{{STRUCTURE_1fhe| PDB=1fhe |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhe OCA], [https://pdbe.org/1fhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhe RCSB], [https://www.ebi.ac.uk/pdbsum/1fhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GST27_FASHE GST27_FASHE] 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/fh/1fhe_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=1fhe ConSurf].
<div style="clear:both"></div>


'''GLUTATHIONE TRANSFERASE (FH47) FROM FASCIOLA HEPATICA'''
==See Also==
 
*[[Glutathione S-transferase|Glutathione S-transferase]]
 
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
==Overview==
__TOC__
Glutathione S-transferases (GSTs) represent the major class of detoxifying enzymes from parasitic helminths. As a result, they are candidates for chemotherapeutic and vaccine design. Indeed, GSTs from Fasciola hepatica have been found to be effective for vaccinating sheep and cattle against fasciolosis. This helminth contains at least seven GST isoforms, of which four have been cloned. The cloned isoforms (Fh51, Fh47, Fh7 and Fh1) all belong to the mu class of GSTs, share greater than 71% sequence identity, yet display distinct substrate specificities. Crystals of Fh47 were obtained using the hanging drop vapour diffusion technique. The crystals belong to space group I4122, with one monomer in the asymmetric unit, which corresponds to a very high solvent content of approximately 75%. The physiological dimer is generated via a crystallographic 2-fold rotation. The three-dimensional structure of Fh47 was solved by molecular replacement using the Schistosoma japonicum glutathione S-transferase (Sj26) crystal structure as a search model. The structure adopts the canonical GST fold comprising two domains: an N-terminal glutathione-binding domain, consisting of a four-stranded beta-sheet and three helices whilst the C-terminal domain is entirely alpha-helical. The presence of Phe19 in Fh47 results in a 6 degrees interdomain rotation in comparison to Sj26, where the equivalent residue is a leucine. Homology models of Fh51, Fh7 and Fh1, based on the Fh47 crystal structure, reveal critical differences in the residues lining the xenobiotic binding site, particularly at residue positions 9, 106 and 204. In addition, differences amongst the isoforms in the non-substrate binding site were noted, which may explain the observed differential binding of large ligands. The major immunogenic epitopes of Fh47 were surprisingly found not to reside on the most solvent-exposed regions of the molecule.Copyright 1997 Academic Press Limited
</StructureSection>
 
==About this Structure==
1FHE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fasciola_hepatica Fasciola hepatica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHE OCA].
 
==Reference==
Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase., Rossjohn J, Feil SC, Wilce MC, Sexton JL, Spithill TW, Parker MW, J Mol Biol. 1997 Nov 7;273(4):857-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9367777 9367777]
[[Category: Fasciola hepatica]]
[[Category: Fasciola hepatica]]
[[Category: Glutathione transferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Parker MW]]
[[Category: Parker, M W.]]
[[Category: Rossjohn J]]
[[Category: Rossjohn, J.]]
[[Category: Detoxification]]
[[Category: Glutathione transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:19:36 2008''

Latest revision as of 07:14, 7 February 2024

GLUTATHIONE TRANSFERASE (FH47) FROM FASCIOLA HEPATICA

1fhe, resolution 3.00Å

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