1m0t
From Proteopedia
(New page: 200px<br /><applet load="1m0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m0t, resolution 2.30Å" /> '''Yeast Glutathione Sy...) |
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| - | [[Image:1m0t.jpg|left|200px]]<br /><applet load="1m0t" size=" | + | [[Image:1m0t.jpg|left|200px]]<br /><applet load="1m0t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m0t, resolution 2.30Å" /> | caption="1m0t, resolution 2.30Å" /> | ||
'''Yeast Glutathione Synthase'''<br /> | '''Yeast Glutathione Synthase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glutathione synthase catalyzes the final ATP-dependent step in glutathione | + | Glutathione synthase catalyzes the final ATP-dependent step in glutathione biosynthesis, the formation of glutathione from gamma-glutamylcysteine and glycine. We have determined structures of yeast glutathione synthase in two forms: unbound (2.3 A resolution) and bound to its substrate gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions (1.8 A resolution). These structures reveal that upon substrate binding, large domain motions convert the enzyme from an open unliganded form to a closed conformation in which protein domains completely surround the substrate in the active site. |
==About this Structure== | ==About this Structure== | ||
| - | 1M0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] Full crystallographic information is available from [http:// | + | 1M0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Gogos, A.]] | [[Category: Gogos, A.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Shapiro, L.]] | [[Category: Shapiro, L.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:16 2008'' |
Revision as of 11:50, 21 February 2008
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Yeast Glutathione Synthase
Overview
Glutathione synthase catalyzes the final ATP-dependent step in glutathione biosynthesis, the formation of glutathione from gamma-glutamylcysteine and glycine. We have determined structures of yeast glutathione synthase in two forms: unbound (2.3 A resolution) and bound to its substrate gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions (1.8 A resolution). These structures reveal that upon substrate binding, large domain motions convert the enzyme from an open unliganded form to a closed conformation in which protein domains completely surround the substrate in the active site.
About this Structure
1M0T is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Glutathione synthase, with EC number 6.3.2.3 Full crystallographic information is available from OCA.
Reference
Large conformational changes in the catalytic cycle of glutathione synthase., Gogos A, Shapiro L, Structure. 2002 Dec;10(12):1669-76. PMID:12467574
Page seeded by OCA on Thu Feb 21 13:50:16 2008
Categories: Glutathione synthase | Saccharomyces cerevisiae | Single protein | Burley, S K. | Gogos, A. | NYSGXRC, New York Structural GenomiX Research Consortium. | Shapiro, L. | SO4 | Amine/carboxylate ligase | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
