2ab6: Difference between revisions

Revision as of 17:25, 21 February 2008

HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE

OverviewOverview

Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and the protein isolated from human tissue were indistinguishable based on physicochemical, enzymatic and immunological criteria. The catalytically active dimeric hGSTM2-2 was crystallized without GSH or other active-site ligands in two crystal forms. Diffraction from form A crystals extends to 2.5 A and is consistent with the space group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two monomers in the asymmetric unit. Diffraction from form B crystals extends to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c = 225.9 A) with two dimers in the asymmetric unit. This is the first report of ligand-free mu-class GST crystals, and a comparison with liganded complexes will provide insight into the structural consequences of substrate binding which are thought to be important for catalysis.

About this StructureAbout this Structure

2AB6 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.

ReferenceReference

Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2., Patskovska LN, Fedorov AA, Patskovsky YV, Almo SC, Listowsky I, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):458-60. PMID:9761928

Page seeded by OCA on Thu Feb 21 16:25:43 2008

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OCA

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-[[Image:2ab6.gif|left|200px]]<br />
+[[Image:2ab6.gif|left|200px]]<br /><applet load="2ab6" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2ab6" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2ab6, resolution 2.50&Aring;" />
 '''HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE'''<br />
 ==Overview==
-Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in, Escherichia coli and purified by GSH-affinity chromatography. The, recombinant enzyme and the protein isolated from human tissue were, indistinguishable based on physicochemical, enzymatic and immunological, criteria. The catalytically active dimeric hGSTM2-2 was crystallized, without GSH or other active-site ligands in two crystal forms. Diffraction, from form A crystals extends to 2.5 A and is consistent with the space, group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two, monomers in the asymmetric unit. Diffraction from form B crystals extends, to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c, = 225.9 A) with two dimers in the asymmetric unit. This is the first, report of ligand-free mu-class GST crystals, and a comparison with, liganded complexes will provide insight into the structural consequences, of substrate binding which are thought to be important for catalysis.
+Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and the protein isolated from human tissue were indistinguishable based on physicochemical, enzymatic and immunological criteria. The catalytically active dimeric hGSTM2-2 was crystallized without GSH or other active-site ligands in two crystal forms. Diffraction from form A crystals extends to 2.5 A and is consistent with the space group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two monomers in the asymmetric unit. Diffraction from form B crystals extends to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c = 225.9 A) with two dimers in the asymmetric unit. This is the first report of ligand-free mu-class GST crystals, and a comparison with liganded complexes will provide insight into the structural consequences of substrate binding which are thought to be important for catalysis.
 ==About this Structure==
-AB6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GSM 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AB6 OCA].
+AB6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GSM:'>GSM</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AB6 OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Almo, S.C.]]
+[[Category: Almo, S C.]]
 [[Category: Listowsky, I.]]
 [[Category: Patskovsky, Y.]]
@@ Line 24: / Line 23: @@
 [[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:48:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:43 2008''