View source for 6gzf


==Xi Class GST from Natrialba magadii==
<StructureSection load='6gzf' size='340' side='right' caption='[[6gzf]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gzf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GZF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gzf OCA], [http://pdbe.org/6gzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gzf RCSB], [http://www.ebi.ac.uk/pdbsum/6gzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gzf ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Xi class glutathione transferases (GSTs) are a recently identified group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea and here we focus on the enzyme produced by the extreme haloalkaliphilic archaeon Natrialba magadii (NmGHR). We investigated its function and stability and determined its 3D structure in the apo form by X-ray crystallography. NmGHR displays the same fold of its mesophilic counterparts, is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. A distinctive feature of haloalkaliphilic archaea is their preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. Indeed we found that the N. magadii genome lacks a gene coding for glutathione synthase. Analysis of NmGHR structure suggests that the thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine.

Structural Characterization of the Xi Class Glutathione Transferase From the Haloalkaliphilic Archaeon Natrialba magadii.,Di Matteo A, Federici L, Masulli M, Carletti E, Santorelli D, Cassidy J, Paradisi F, Di Ilio C, Allocati N Front Microbiol. 2019 Jan 18;10:9. doi: 10.3389/fmicb.2019.00009. eCollection, 2019. PMID:30713525<ref>PMID:30713525</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gzf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glutathione transferase]]
[[Category: Allocati, N]]
[[Category: Carletti, E]]
[[Category: Cassidy, J]]
[[Category: Federici, L]]
[[Category: Ilio, C Di]]
[[Category: Masulli, M]]
[[Category: Matteo, A Di]]
[[Category: Paradisi, F]]
[[Category: Extremozyme]]
[[Category: Glutathionyl-hydroquinone reductase]]
[[Category: Natrialba magadii]]
[[Category: Transferase]]