2io7: Difference between revisions
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<StructureSection load='2io7' size='340' side='right'caption='[[2io7]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2io7' size='340' side='right'caption='[[2io7]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2io7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2io7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IO7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2io8|2io8]], [[2io9|2io9]], [[2ioa|2ioa]], [[2iob|2iob]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2io8|2io8]], [[2io9|2io9]], [[2ioa|2ioa]], [[2iob|2iob]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2io7 OCA], [https://pdbe.org/2io7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2io7 RCSB], [https://www.ebi.ac.uk/pdbsum/2io7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2io7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/GSP_ECOLI GSP_ECOLI]] Catalyzes the formation of an amide bond between glutathione and spermidine coupled with hydrolysis of ATP; also catalyzes the hydrolysis of glutathionylspermidine to glutathione and spermidine. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:29, 12 January 2022
E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNPE. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ and AMPPNP
Structural highlights
Function[GSP_ECOLI] Catalyzes the formation of an amide bond between glutathione and spermidine coupled with hydrolysis of ATP; also catalyzes the hydrolysis of glutathionylspermidine to glutathione and spermidine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMost 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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