3gx0: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='3gx0' size='340' side='right'caption='[[3gx0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3gx0' size='340' side='right'caption='[[3gx0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3gx0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GX0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3gx0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GX0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yfcG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gx0 OCA], [https://pdbe.org/3gx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gx0 RCSB], [https://www.ebi.ac.uk/pdbsum/3gx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gx0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gx0 OCA], [https://pdbe.org/3gx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gx0 RCSB], [https://www.ebi.ac.uk/pdbsum/3gx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gx0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/YFCG_ECOLI YFCG_ECOLI]] Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:17018556</ref> <ref>PMID:19537707</ref>
[https://www.uniprot.org/uniprot/YFCG_ECOLI YFCG_ECOLI] Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:17018556</ref> <ref>PMID:19537707</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</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=3gx0 ConSurf].
</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=3gx0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
YfcG is one of eight glutathione (GSH) transferase homologues encoded in the Escherichia coli genome. The protein exhibits low or no GSH transferase activity toward a panel of electrophilic substrates. In contrast, it has a very robust disulfide-bond reductase activity toward 2-hydroxyethyldisulfide on par with mammalian and bacterial glutaredoxins. The structure of YfcG at 2.3 A-resolution from crystals grown in the presence of GSH reveals a molecule of glutathione disulfide in the active site. The crystallographic results and the lack of functional cysteine residues in the active site of YfcG suggests that the reductase activity is unique in that no sulfhydryl groups in the YfcG protein are covalently involved in the redox chemistry.
Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase.,Wadington MC, Ladner JE, Stourman NV, Harp JM, Armstrong RN Biochemistry. 2009 Jun 23. PMID:19537707<ref>PMID:19537707</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3gx0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Armstrong, R N]]
[[Category: Armstrong RN]]
[[Category: Harp, J M]]
[[Category: Harp JM]]
[[Category: Ladner, J E]]
[[Category: Ladner JE]]
[[Category: Wadington, M C]]
[[Category: Wadington MC]]
[[Category: Disulfide bond oxidoreductase]]
[[Category: Glutathione]]
[[Category: Glutathione disulfide]]
[[Category: Transferase]]

Latest revision as of 09:57, 21 February 2024

Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase

3gx0, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3gx0&oldid=4065131"