1mpg
From Proteopedia
(New page: 200px<br /><applet load="1mpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpg, resolution 1.80Å" /> '''3-METHYLADENINE DNA ...) |
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| - | [[Image:1mpg.gif|left|200px]]<br /><applet load="1mpg" size=" | + | [[Image:1mpg.gif|left|200px]]<br /><applet load="1mpg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mpg, resolution 1.80Å" /> | caption="1mpg, resolution 1.80Å" /> | ||
'''3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI'''<br /> | '''3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Base-excision DNA repair proteins that target alkylation damage act on a | + | Base-excision DNA repair proteins that target alkylation damage act on a variety of seemingly dissimilar adducts, yet fail to recognize other closely related lesions. The 1.8 A crystal structure of the monofunctional DNA glycosylase AlkA (E. coli 3-methyladenine-DNA glycosylase II) reveals a large hydrophobic cleft unusually rich in aromatic residues. An Asp residue projecting into this cleft is essential for catalysis, and it governs binding specificity for mechanism-based inhibitors. We propose that AlkA recognizes electron-deficient methylated bases through pi-donor/acceptor interactions involving the electron-rich aromatic cleft. Remarkably, AlkA is similar in fold and active site location to the bifunctional glycosylase/lyase endonuclease III, suggesting the two may employ fundamentally related mechanisms for base excision. |
==About this Structure== | ==About this Structure== | ||
| - | 1MPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1MPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1MPG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ellenberger, T | + | [[Category: Ellenberger, T E.]] |
[[Category: Ezaz-Nikpay, K.]] | [[Category: Ezaz-Nikpay, K.]] | ||
[[Category: Labahn, J.]] | [[Category: Labahn, J.]] | ||
[[Category: Long, A.]] | [[Category: Long, A.]] | ||
| - | [[Category: Schaerer, O | + | [[Category: Schaerer, O D.]] |
| - | [[Category: Verdine, G | + | [[Category: Verdine, G L.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: alka]] | [[Category: alka]] | ||
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[[Category: methylation]] | [[Category: methylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:39 2008'' |
Revision as of 11:57, 21 February 2008
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3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI
Overview
Base-excision DNA repair proteins that target alkylation damage act on a variety of seemingly dissimilar adducts, yet fail to recognize other closely related lesions. The 1.8 A crystal structure of the monofunctional DNA glycosylase AlkA (E. coli 3-methyladenine-DNA glycosylase II) reveals a large hydrophobic cleft unusually rich in aromatic residues. An Asp residue projecting into this cleft is essential for catalysis, and it governs binding specificity for mechanism-based inhibitors. We propose that AlkA recognizes electron-deficient methylated bases through pi-donor/acceptor interactions involving the electron-rich aromatic cleft. Remarkably, AlkA is similar in fold and active site location to the bifunctional glycosylase/lyase endonuclease III, suggesting the two may employ fundamentally related mechanisms for base excision.
About this Structure
1MPG is a Single protein structure of sequence from Escherichia coli with as ligand. Active as DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 Full crystallographic information is available from OCA.
Reference
Structural basis for the excision repair of alkylation-damaged DNA., Labahn J, Scharer OD, Long A, Ezaz-Nikpay K, Verdine GL, Ellenberger TE, Cell. 1996 Jul 26;86(2):321-9. PMID:8706136
Page seeded by OCA on Thu Feb 21 13:57:39 2008
