1mwj: Difference between revisions
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[[Image:1mwj.gif|left|200px]] | [[Image:1mwj.gif|left|200px]] | ||
'''Crystal Structure of a MUG-DNA pseudo substrate complex''' | {{Structure | ||
|PDB= 1mwj |SIZE=350|CAPTION= <scene name='initialview01'>1mwj</scene>, resolution 2.85Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= MUG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal Structure of a MUG-DNA pseudo substrate complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MWJ is a [ | 1MWJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWJ OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a thwarted mismatch glycosylase DNA repair complex., Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH, EMBO J. 1999 Dec 1;18(23):6599-609. PMID:[http:// | Crystal structure of a thwarted mismatch glycosylase DNA repair complex., Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH, EMBO J. 1999 Dec 1;18(23):6599-609. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10581234 10581234] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: uracil recognition.]] | [[Category: uracil recognition.]] | ||
''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 12:49:04 2008'' | ||
Revision as of 10:49, 20 March 2008
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| 1mwj, resolution 2.85Å | |||||||||||||
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| Gene: | MUG (Escherichia coli) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of a MUG-DNA pseudo substrate complex
Overview
The bacterial mismatch-specific uracil-DNA glycosylase (MUG) and eukaryotic thymine-DNA glycosylase (TDG) enzymes form a homologous family of DNA glycosylases that initiate base-excision repair of G:U/T mismatches. Despite low sequence homology, the MUG/TDG enzymes are structurally related to the uracil-DNA glycosylase enzymes, but have a very different mechanism for substrate recognition. We have now determined the crystal structure of the Escherichia coli MUG enzyme complexed with an oligonucleotide containing a non-hydrolysable deoxyuridine analogue mismatched with guanine, providing the first structure of an intact substrate-nucleotide productively bound to a hydrolytic DNA glycosylase. The structure of this complex explains the preference for G:U over G:T mispairs, and reveals an essentially non-specific pyrimidine-binding pocket that allows MUG/TDG enzymes to excise the alkylated base, 3, N(4)-ethenocytosine. Together with structures for the free enzyme and for an abasic-DNA product complex, the MUG-substrate analogue complex reveals the conformational changes accompanying the catalytic cycle of substrate binding, base excision and product release.
About this Structure
1MWJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of a thwarted mismatch glycosylase DNA repair complex., Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH, EMBO J. 1999 Dec 1;18(23):6599-609. PMID:10581234
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