2io7: Difference between revisions

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[[Image:2io7.jpg|left|200px]]
[[Image:2io7.jpg|left|200px]]


{{Structure
<!--
|PDB= 2io7 |SIZE=350|CAPTION= <scene name='initialview01'>2io7</scene>, resolution 2.7&Aring;
The line below this paragraph, containing "STRUCTURE_2io7", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY=  
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|GENE=  
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|DOMAIN=
{{STRUCTURE_2io7| PDB=2io7  | SCENE= }}  
|RELATEDENTRY=[[2io8|2IO8]], [[2io9|2IO9]], [[2ioa|2IOA]], [[2iob|2IOB]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2io7 OCA], [http://www.ebi.ac.uk/pdbsum/2io7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2io7 RCSB]</span>
}}


'''E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNP'''
'''E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNP'''
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[[Category: Wang, A H.J.]]
[[Category: Wang, A H.J.]]
[[Category: Yen, F J.]]
[[Category: Yen, F J.]]
[[Category: bifunctional glutathionylspermidine synthetase/amidase]]
[[Category: Bifunctional glutathionylspermidine synthetase/amidase]]
 
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Revision as of 07:42, 4 May 2008

File:2io7.jpg

Template:STRUCTURE 2io7

E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNP


OverviewOverview

Most organisms use glutathione to regulate intracellular thiol redox balance and protect against oxidative stress; protozoa, however, utilize trypanothione for this purpose. Trypanothione biosynthesis requires ATP-dependent conjugation of glutathione (GSH) to the two terminal amino groups of spermidine by glutathionylspermidine synthetase (GspS) and trypanothione synthetase (TryS), which are considered as drug targets. GspS catalyzes the penultimate step of the biosynthesis-amide bond formation between spermidine and the glycine carboxylate of GSH. We report herein five crystal structures of Escherichia coli GspS in complex with substrate, product or inhibitor. The C-terminal of GspS belongs to the ATP-grasp superfamily with a similar fold to the human glutathione synthetase. GSH is likely phosphorylated at one of two GSH-binding sites to form an acylphosphate intermediate that then translocates to the other site for subsequent nucleophilic addition of spermidine. We also identify essential amino acids involved in the catalysis. Our results constitute the first structural information on the biochemical features of parasite homologs (including TryS) that underlie their broad specificity for polyamines.

About this StructureAbout this Structure

2IO7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase., Pai CH, Chiang BY, Ko TP, Chou CC, Chong CM, Yen FJ, Chen S, Coward JK, Wang AH, Lin CH, EMBO J. 2006 Dec 13;25(24):5970-82. Epub 2006 Nov 23. PMID:17124497 Page seeded by OCA on Sun May 4 07:42:47 2008

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