1oe7

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[[Image:1oe7.jpg|left|200px]]<br /><applet load="1oe7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oe7.jpg|left|200px]]
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caption="1oe7, resolution 1.80&Aring;" />
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'''28KDA GLUTATHIONE S-TRANSFERASE FROM SCHISTOSOMA HAEMATOBIUM'''<br />
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{{Structure
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|PDB= 1oe7 |SIZE=350|CAPTION= <scene name='initialview01'>1oe7</scene>, resolution 1.80&Aring;
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|SITE= <scene name='pdbsite=AC1:Gsh+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]
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|GENE=
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}}
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'''28KDA GLUTATHIONE S-TRANSFERASE FROM SCHISTOSOMA HAEMATOBIUM'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OE7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_haematobium Schistosoma haematobium] with <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Known structural/functional Site: <scene name='pdbsite=AC1:Gsh+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE7 OCA].
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1OE7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_haematobium Schistosoma haematobium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE7 OCA].
==Reference==
==Reference==
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Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium., Johnson KA, Angelucci F, Bellelli A, Herve M, Fontaine J, Tsernoglou D, Capron A, Trottein F, Brunori M, Biochemistry. 2003 Sep 2;42(34):10084-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12939136 12939136]
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Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium., Johnson KA, Angelucci F, Bellelli A, Herve M, Fontaine J, Tsernoglou D, Capron A, Trottein F, Brunori M, Biochemistry. 2003 Sep 2;42(34):10084-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12939136 12939136]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Schistosoma haematobium]]
[[Category: Schistosoma haematobium]]
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[[Category: vaccine candidate]]
[[Category: vaccine candidate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:37 2008''

Revision as of 11:09, 20 March 2008


PDB ID 1oe7

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands:
Activity: Glutathione transferase, with EC number 2.5.1.18
Coordinates: save as pdb, mmCIF, xml



28KDA GLUTATHIONE S-TRANSFERASE FROM SCHISTOSOMA HAEMATOBIUM


Overview

Schistomiasis is a debilitating parasitic disease which affects 200 million people, causing life-threatening complications in 10% of the patients. This paper reports the crystal structure of the Schistosoma haematobium 28 kDa glutathione S-transferase, a multifunctional enzyme involved in host-parasite interactions and presently considered as a promising vaccine candidate against schistosomiasis. The structures of the GSH-free enzyme, as well as the partially (approximately 40%) and almost fully (approximately 80%) GSH-saturated enzyme, exhibit a unique feature, absent in previous GST structures, concerning the crucial and invariant Tyr10 side chain which occupies two alternative positions. The canonical conformer, which allows an H-bond to be formed between the side chain hydroxyl group and the activated thiolate of GSH, is somewhat less than 50% occupied. The new conformer, with the phenoxyl ring on the opposite side of the mobile loop connecting strand 1 and helix 1, is stabilized by a polar interaction with the guanidinium group of the conserved Arg21 side chain. The presence of two conformers of Tyr10 may provide a clue about clarifying the multiple catalytic functions of Sh28GST and might prove to be relevant for the design of specific antischistosomal drugs. The K(d) for GSH binding was determined by equilibrium fluorescence titrations to be approximately 3 microM and by stopped-flow rapid mixing experiments to be approximately 9 microM. The relatively tight binding of GSH by Sh28GST explains the residually bound GSH in the crystal and supports a possible role of GSH as a tightly bound cofactor involved in the catalytic mechanism for prostaglandin D(2) synthase activity.

About this Structure

1OE7 is a Single protein structure of sequence from Schistosoma haematobium. Full crystallographic information is available from OCA.

Reference

Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium., Johnson KA, Angelucci F, Bellelli A, Herve M, Fontaine J, Tsernoglou D, Capron A, Trottein F, Brunori M, Biochemistry. 2003 Sep 2;42(34):10084-94. PMID:12939136

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