1bnk
From Proteopedia
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| - | [[Image:1bnk.gif|left|200px]] | + | [[Image:1bnk.gif|left|200px]] |
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| - | '''HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA''' | + | {{Structure |
| + | |PDB= 1bnk |SIZE=350|CAPTION= <scene name='initialview01'>1bnk</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA-3-methyladenine_glycosylase_II DNA-3-methyladenine glycosylase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.21 3.2.2.21] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BNK is a [ | + | 1BNK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNK OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision., Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T, Cell. 1998 Oct 16;95(2):249-58. PMID:[http:// | + | Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision., Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T, Cell. 1998 Oct 16;95(2):249-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9790531 9790531] |
[[Category: DNA-3-methyladenine glycosylase II]] | [[Category: DNA-3-methyladenine glycosylase II]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: dna repair]] | [[Category: dna repair]] | ||
| - | ''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 10:13:20 2008'' |
Revision as of 08:13, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Activity: | DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA
Contents |
Overview
DNA N-glycosylases are base excision-repair proteins that locate and cleave damaged bases from DNA as the first step in restoring the genetic blueprint. The human enzyme 3-methyladenine DNA glycosylase removes a diverse group of damaged bases from DNA, including cytotoxic and mutagenic alkylation adducts of purines. We report the crystal structure of human 3-methyladenine DNA glycosylase complexed to a mechanism-based pyrrolidine inhibitor. The enzyme has intercalated into the minor groove of DNA, causing the abasic pyrrolidine nucleotide to flip into the enzyme active site, where a bound water is poised for nucleophilic attack. The structure shows an elegant means of exposing a nucleotide for base excision as well as a network of residues that could catalyze the in-line displacement of a damaged base from the phosphodeoxyribose backbone.
Disease
Known disease associated with this structure: Opitz G syndrome, type I OMIM:[300552]
About this Structure
1BNK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision., Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T, Cell. 1998 Oct 16;95(2):249-58. PMID:9790531
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