2io7: Difference between revisions

Revision as of 10:08, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2io7.png

Template:STRUCTURE 2io7

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

Template:ABSTRACT PUBMED 17124497

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

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OCA

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-'''E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNP'''
+===E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNP===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17124497}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17124497}}
 ==About this Structure==
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 [[Category: Yen, F J.]]
 [[Category: Bifunctional glutathionylspermidine synthetase/amidase]]
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