View source for 2lwf


==Structure of N-terminal domain of a plant Grx==
<StructureSection load='2lwf' size='340' side='right' caption='[[2lwf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lwf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LWF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LWF FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRXS16, At2g38270, F16M14.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=2lwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lwf OCA], [http://pdbe.org/2lwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lwf RCSB], [http://www.ebi.ac.uk/pdbsum/2lwf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lwf ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GRS16_ARATH GRS16_ARATH]] May only reduce GSH-thiol disulfides, but not protein disulfides (Potential). 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions. A chloroplastic monothiol glutaredoxin, AtGRXS16 from Arabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr-TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulation and DNA cleavage in chloroplasts. Structural determination of AtGRXS16-NTD showed that it possesses a GIY-YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY-YIG endonucleases. AtGRXS16-NTD was able to cleave lambdaDNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel a manner of regulation for Grxs and provide insights into the mechanistic link between redox regulation and DNA metabolism in chloroplasts.

Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.,Liu X, Liu S, Feng Y, Liu JZ, Chen Y, Pham K, Deng H, Hirschi KD, Wang X, Cheng N Proc Natl Acad Sci U S A. 2013 May 20. PMID:23690600<ref>PMID:23690600</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lwf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Feng, Y]]
[[Category: Glutaredoxin]]
[[Category: Hydrolase]]
[[Category: Nuclease]]