1nku
From Proteopedia
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|PDB= 1nku |SIZE=350|CAPTION= <scene name='initialview01'>1nku</scene> | |PDB= 1nku |SIZE=350|CAPTION= <scene name='initialview01'>1nku</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lmz|1LMZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nku OCA], [http://www.ebi.ac.uk/pdbsum/1nku PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nku RCSB]</span> | ||
}} | }} | ||
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[[Category: Kwon, K.]] | [[Category: Kwon, K.]] | ||
[[Category: Stivers, J T.]] | [[Category: Stivers, J T.]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:47 2008'' |
Revision as of 19:31, 30 March 2008
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| Ligands: | |||||||
| Activity: | DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 | ||||||
| Related: | 1LMZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 22:31:47 2008
