View source for 4tr1


==Crystal structure of GSH-bound cGrx2/C15S==
<StructureSection load='4tr1' size='340' side='right'caption='[[4tr1]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4tr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkaliphilus_oremlandii_OhILAs Alkaliphilus oremlandii OhILAs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TR1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.582&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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=4tr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tr1 OCA], [https://pdbe.org/4tr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4tr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tr1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8MJH2_ALKOO A8MJH2_ALKOO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutaredoxin (Grx) is a major redox enzyme that reduces disulfide bonds using glutathione (GSH) as an electron donor. The anaerobic bacterium Clostridium oremlandii possesses a selenocysteine-containing Grx (cGrx1) and a cysteine-containing homolog (cGrx2). Here, the crystal structure of the GSSG-bound form of cGrx2 was determined for the first time at a resolution of 1.95 A. In addition, its monothiol variant cGrx2/C15S in complex with GSH was also determined at a resolution of 1.58 A. cGrx2 is a monomeric protein with an overall structure that consists of the typical thioredoxin fold composed of four alpha-helices and four beta-strands. Two ligands, GSH and GSSG, share a conserved binding site consisting of CPYC, TVP, and CDD motifs. The cysteinyl and gamma-glutamyl moieties show similar binding interactions in the two structures, whereas the glycine moiety shows different interactions. Interestingly, the structures revealed that only one GSH moiety of GSSG is sufficient for its binding to the protein. The GSSG-bound structure of cGrx2 was obtained as an oxidized form with a disulfide bond at the CPYC motif. Comparison of the GSH-binding mode in cGrx2 to other known Grxs revealed similarities as well as some diversity.

The GSH- and GSSG-bound structures of glutaredoxin from Clostridium oremlandii.,Lee EH, Kim HY, Hwang KY Arch Biochem Biophys. 2014 Sep 9. pii: S0003-9861(14)00320-8. doi:, 10.1016/j.abb.2014.09.001. PMID:25218089<ref>PMID:25218089</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4tr1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alkaliphilus oremlandii OhILAs]]
[[Category: Large Structures]]
[[Category: Hwang KY]]
[[Category: Lee EH]]