2LWF
Structure of N-terminal domain of a plant Grx
Summary for 2LWF
| Entry DOI | 10.2210/pdb2lwf/pdb |
| NMR Information | BMRB: 18624 |
| Descriptor | Monothiol glutaredoxin-S16, chloroplastic (1 entity in total) |
| Functional Keywords | nuclease, glutaredoxin, hydrolase |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Cellular location | Plastid, chloroplast (Potential): Q8H7F6 |
| Total number of polymer chains | 1 |
| Total formula weight | 12907.64 |
| Authors | Feng, Y. (deposition date: 2012-07-28, release date: 2013-05-22, Last modification date: 2024-05-15) |
| Primary citation | Liu, X.,Liu, S.,Feng, Y.,Liu, J.Z.,Chen, Y.,Pham, K.,Deng, H.,Hirschi, K.D.,Wang, X.,Cheng, N. Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts. Proc.Natl.Acad.Sci.USA, 110:9565-9570, 2013 Cited by PubMed Abstract: 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 λDNA 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. PubMed: 23690600DOI: 10.1073/pnas.1306899110 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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