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1lmz
From Proteopedia
(New page: 200px<br /><applet load="1lmz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lmz" /> '''Solution Structure of 3-Methyladenine DNA Gl...) |
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| - | [[Image:1lmz.gif|left|200px]]<br /><applet load="1lmz" size=" | + | [[Image:1lmz.gif|left|200px]]<br /><applet load="1lmz" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)'''<br /> | '''Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Escherichia coli enzyme 3-methyladenine DNA glycosylase I (TAG) | + | The Escherichia coli enzyme 3-methyladenine DNA glycosylase I (TAG) hydrolyzes the glycosidic bond of 3-methyladenine (3-MeA) in DNA and is found in many bacteria and some higher eukaryotes. TAG shows little primary sequence identity with members of the well-known helix-hairpin-helix (HhH) superfamily of DNA repair glycosylases, which consists of AlkA, EndoIII, MutY and hOGG1. Unexpectedly, the three-dimensional solution structure reported here reveals TAG as member of this superfamily. The restricted specificity of TAG for 3-MeA bases probably arises from its unique aromatic rich 3-MeA binding pocket and the absence of a catalytic aspartate that is present in all other HhH family members. |
==About this Structure== | ==About this Structure== | ||
| - | 1LMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http:// | + | 1LMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Drohat, A | + | [[Category: Drohat, A C.]] |
| - | [[Category: Krosky, D | + | [[Category: Krosky, D J.]] |
[[Category: Kwon, K.]] | [[Category: Kwon, K.]] | ||
| - | [[Category: Stivers, J | + | [[Category: Stivers, J T.]] |
[[Category: 3-methyladenine]] | [[Category: 3-methyladenine]] | ||
[[Category: dna glycosylase]] | [[Category: dna glycosylase]] | ||
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[[Category: tag]] | [[Category: tag]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:25 2008'' |
Revision as of 11:46, 21 February 2008
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Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)
Overview
The Escherichia coli enzyme 3-methyladenine DNA glycosylase I (TAG) hydrolyzes the glycosidic bond of 3-methyladenine (3-MeA) in DNA and is found in many bacteria and some higher eukaryotes. TAG shows little primary sequence identity with members of the well-known helix-hairpin-helix (HhH) superfamily of DNA repair glycosylases, which consists of AlkA, EndoIII, MutY and hOGG1. Unexpectedly, the three-dimensional solution structure reported here reveals TAG as member of this superfamily. The restricted specificity of TAG for 3-MeA bases probably arises from its unique aromatic rich 3-MeA binding pocket and the absence of a catalytic aspartate that is present in all other HhH family members.
About this Structure
1LMZ is a Single protein structure of sequence from Escherichia coli. Active as DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 Full crystallographic information is available from OCA.
Reference
3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member., Drohat AC, Kwon K, Krosky DJ, Stivers JT, Nat Struct Biol. 2002 Sep;9(9):659-64. PMID:12161745
Page seeded by OCA on Thu Feb 21 13:46:25 2008
