1nku

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[[Image:1nku.gif|left|200px]]
[[Image:1nku.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1nku |SIZE=350|CAPTION= <scene name='initialview01'>1nku</scene>
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The line below this paragraph, containing "STRUCTURE_1nku", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1nku| PDB=1nku | SCENE= }}
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|RELATEDENTRY=[[1lmz|1LMZ]]
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|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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}}
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'''NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)'''
'''NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)'''
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[[Category: Kwon, K.]]
[[Category: Kwon, K.]]
[[Category: Stivers, J T.]]
[[Category: Stivers, J T.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:39:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:47 2008''
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Revision as of 23:39, 2 May 2008

Image:1nku.gif

Template:STRUCTURE 1nku

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 Sat May 3 02:39:07 2008

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