2iob: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2iob.jpg|left|200px]]


{{Structure
==E. coli Bifunctional glutathionylspermidine synthetase/amidase Apo protein==
|PDB= 2iob |SIZE=350|CAPTION= <scene name='initialview01'>2iob</scene>, resolution 2.2&Aring;
<StructureSection load='2iob' size='340' side='right'caption='[[2iob]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2iob]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IOB FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iob OCA], [https://pdbe.org/2iob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iob RCSB], [https://www.ebi.ac.uk/pdbsum/2iob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iob ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[2io7|2IO7]], [[2io8|2IO8]], [[2io9|2IO9]], [[2ioa|2IOA]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iob OCA], [http://www.ebi.ac.uk/pdbsum/2iob PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iob RCSB]</span>
[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 ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''E. coli Bifunctional glutathionylspermidine synthetase/amidase Apo protein'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/2iob_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2iob ConSurf].
2IOB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOB OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
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:[http://www.ncbi.nlm.nih.gov/pubmed/17124497 17124497]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chiang, B Y.]]
[[Category: Chiang BY]]
[[Category: Chong, C M.]]
[[Category: Chong CM]]
[[Category: Chou, C C.]]
[[Category: Chou CC]]
[[Category: Coward, J K.]]
[[Category: Coward JK]]
[[Category: Ko, T P.]]
[[Category: Ko TP]]
[[Category: Lin, C H.]]
[[Category: Lin CH]]
[[Category: Pai, C H.]]
[[Category: Pai CH]]
[[Category: Wang, A H.J.]]
[[Category: Wang AH-J]]
[[Category: Yen, F J.]]
[[Category: Yen FJ]]
[[Category: bifunctional glutathionylspermidine synthetase/amidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:46:45 2008''

Latest revision as of 16:52, 13 March 2024

E. coli Bifunctional glutathionylspermidine synthetase/amidase Apo proteinE. coli Bifunctional glutathionylspermidine synthetase/amidase Apo protein

Structural highlights

2iob is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

2iob, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA