1nku
From Proteopedia
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| - | [[Image:1nku.gif|left|200px]] | + | [[Image:1nku.gif|left|200px]] |
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| - | '''NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)''' | + | {{Structure |
| + | |PDB= 1nku |SIZE=350|CAPTION= <scene name='initialview01'>1nku</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA-3-methyladenine_glycosylase_I DNA-3-methyladenine glycosylase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.20 3.2.2.20] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NKU is a [ | + | 1NKU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKU OCA]. |
==Reference== | ==Reference== | ||
| - | A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I., Kwon K, Cao C, Stivers JT, J Biol Chem. 2003 May 23;278(21):19442-6. Epub 2003 Mar 24. PMID:[http:// | + | A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I., Kwon K, Cao C, Stivers JT, J Biol Chem. 2003 May 23;278(21):19442-6. Epub 2003 Mar 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12654914 12654914] |
[[Category: DNA-3-methyladenine glycosylase I]] | [[Category: DNA-3-methyladenine glycosylase I]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:08 2008'' |
Revision as of 10:58, 20 March 2008
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| Ligands: | |||||||
| Activity: | DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)
Overview
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.
About this Structure
1NKU is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I., Kwon K, Cao C, Stivers JT, J Biol Chem. 2003 May 23;278(21):19442-6. Epub 2003 Mar 24. PMID:12654914
Page seeded by OCA on Thu Mar 20 12:58:08 2008
