1NKU
NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)
Summary for 1NKU
| Entry DOI | 10.2210/pdb1nku/pdb |
| Related | 1LMZ |
| NMR Information | BMRB: 5668 |
| Descriptor | 3-Methyladenine Dna Glycosylase I (TAG), ZINC ION (2 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 21203.54 |
| Authors | Kwon, K.,Cao, C.,Stivers, J.T. (deposition date: 2003-01-03, release date: 2003-06-03, Last modification date: 2024-05-22) |
| Primary citation | Kwon, K.,Cao, C.,Stivers, J.T. A Novel Zinc Snap Motif Conveys Structural Stability to 3-Methyladenine DNA Glycosylase I J.Biol.Chem., 278:19442-19446, 2003 Cited by PubMed Abstract: The Escherichia coli 3-methyladenine DNA glycosylase I (TAG) is a DNA repair enzyme that excises 3-methyladenine in DNA and is the smallest member of the helix-hairpin-helix (HhH) superfamily of DNA glycosylases. Despite many studies over the last 25 years, there has been no suggestion that TAG was a metalloprotein. However, here we establish by heteronuclear NMR and other spectroscopic methods that TAG binds 1 eq of Zn2+ extremely tightly. A family of refined NMR structures shows that 4 conserved residues contributed from the amino- and carboxyl-terminal regions of TAG (Cys4, His17, His175, and Cys179) form a Zn2+ binding site. The Zn2+ ion serves to tether the otherwise unstructured amino- and carboxyl-terminal regions of TAG. We propose that this unexpected "zinc snap" motif in the TAG family (CX(12-17)HX(approximately 150)HX(3)C) serves to stabilize the HhH domain thereby mimicking the functional role of protein-protein interactions in larger HhH superfamily members. PubMed: 12654914DOI: 10.1074/jbc.M300934200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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