1bnk

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(New page: 200px<br /> <applet load="1bnk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bnk, resolution 2.7&Aring;" /> '''HUMAN 3-METHYLADENIN...)
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'''HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA'''<br />
'''HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1BNK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BNK OCA].
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1BNK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNK OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger, T.]]
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[[Category: Lau, A.Y.]]
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[[Category: Lau, A Y.]]
[[Category: Samson, L.]]
[[Category: Samson, L.]]
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[[Category: Schaerer, O.D.]]
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[[Category: Schaerer, O D.]]
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[[Category: Verdine, G.L.]]
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[[Category: Verdine, G L.]]
[[Category: dna glycosylase]]
[[Category: dna glycosylase]]
[[Category: dna repair]]
[[Category: dna repair]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:05 2008''

Revision as of 09:57, 21 February 2008


1bnk, resolution 2.7Å

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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. Active as DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 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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