2io7
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2io7 |SIZE=350|CAPTION= <scene name='initialview01'>2io7</scene>, resolution 2.7Å | |PDB= 2io7 |SIZE=350|CAPTION= <scene name='initialview01'>2io7</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |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> | ||
}} | }} | ||
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[[Category: Wang, A H.J.]] | [[Category: Wang, A H.J.]] | ||
[[Category: Yen, F J.]] | [[Category: Yen, F J.]] | ||
| - | [[Category: ANP]] | ||
| - | [[Category: MG]] | ||
[[Category: bifunctional glutathionylspermidine synthetase/amidase]] | [[Category: bifunctional glutathionylspermidine synthetase/amidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:46:49 2008'' |
Revision as of 00:46, 31 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 2IO8, 2IO9, 2IOA, 2IOB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
2IO7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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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