1lmz
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |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= TAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= TAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmz OCA], [http://www.ebi.ac.uk/pdbsum/1lmz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lmz RCSB]</span> | ||
}} | }} | ||
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[[Category: tag]] | [[Category: tag]] | ||
| - | ''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 22:04:44 2008'' |
Revision as of 19:04, 30 March 2008
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| Gene: | TAG (Escherichia coli) | ||||||
| Activity: | DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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