6mws

From Proteopedia

(Difference between revisions)

Current revision

crystal structure of the reduced Grx1 from Saccharomyces cerevisiae

Structural highlights

6mws is a 1 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	GRX1, YCL035C, YCL35C (Baker's yeast)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLRX1_YEAST] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Grx1, a cytosolic thiol-disulfide oxidoreductase, actively maintains cellular redox homeostasis using glutathione substrates (reduced, GSH, and oxidized, GSSG). Here, the crystallization of reduced Grx1 from the yeast Saccharomyces cerevisiae (yGrx1) in space group P212121 and its structure solution and refinement to 1.22 A resolution are reported. To study the structure-function relationship of yeast Grx1, the crystal structure of reduced yGrx1 was compared with the existing structures of the oxidized and glutathionylated forms. These comparisons revealed structural differences in the conformations of residues neighbouring the Cys27-Cys30 active site which accompany alterations in the redox status of the protein.

High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.,Maghool S, La Fontaine S, Maher MJ Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):392-396. doi:, 10.1107/S2053230X19003327. Epub 2019 Apr 26. PMID:31045569^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Luikenhuis S, Perrone G, Dawes IW, Grant CM. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell. 1998 May;9(5):1081-91. PMID:9571241
↑ Collinson EJ, Wheeler GL, Garrido EO, Avery AM, Avery SV, Grant CM. The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem. 2002 May 10;277(19):16712-7. Epub 2002 Mar 1. PMID:11875065 doi:http://dx.doi.org/10.1074/jbc.M111686200
↑ Collinson EJ, Grant CM. Role of yeast glutaredoxins as glutathione S-transferases. J Biol Chem. 2003 Jun 20;278(25):22492-7. Epub 2003 Apr 8. PMID:12684511 doi:http://dx.doi.org/10.1074/jbc.M301387200
↑ Maghool S, La Fontaine S, Maher MJ. High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):392-396. doi:, 10.1107/S2053230X19003327. Epub 2019 Apr 26. PMID:31045569 doi:http://dx.doi.org/10.1107/S2053230X19003327

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6mws"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6mws is ON HOLD
+==crystal structure of the reduced Grx1 from Saccharomyces cerevisiae==
+<StructureSection load='6mws' size='340' side='right'caption='[[6mws]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6mws]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MWS 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX1, YCL035C, YCL35C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=6mws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mws OCA], [http://pdbe.org/6mws PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mws RCSB], [http://www.ebi.ac.uk/pdbsum/6mws PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mws ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GLRX1_YEAST GLRX1_YEAST]] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.<ref>PMID:9571241</ref> <ref>PMID:11875065</ref> <ref>PMID:12684511</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Grx1, a cytosolic thiol-disulfide oxidoreductase, actively maintains cellular redox homeostasis using glutathione substrates (reduced, GSH, and oxidized, GSSG). Here, the crystallization of reduced Grx1 from the yeast Saccharomyces cerevisiae (yGrx1) in space group P212121 and its structure solution and refinement to 1.22 A resolution are reported. To study the structure-function relationship of yeast Grx1, the crystal structure of reduced yGrx1 was compared with the existing structures of the oxidized and glutathionylated forms. These comparisons revealed structural differences in the conformations of residues neighbouring the Cys27-Cys30 active site which accompany alterations in the redox status of the protein.
-Authors:
+High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.,Maghool S, La Fontaine S, Maher MJ Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):392-396. doi:, 10.1107/S2053230X19003327. Epub 2019 Apr 26. PMID:31045569<ref>PMID:31045569</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6mws" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Baker's yeast]]
+[[Category: Large Structures]]
+[[Category: Maghool, S]]
+[[Category: Maher, J M]]
+[[Category: Glutaredoxin 1]]
+[[Category: Oxidoreductase]]
+[[Category: Yeast saccharomyces cerevisiae]]

6mws

From Proteopedia

Current revision

crystal structure of the reduced Grx1 from Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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