1mpg
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
- | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= ALKA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ALKA ([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=1mpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpg OCA], [http://www.ebi.ac.uk/pdbsum/1mpg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mpg RCSB]</span> | ||
}} | }} | ||
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[[Category: Schaerer, O D.]] | [[Category: Schaerer, O D.]] | ||
[[Category: Verdine, G L.]] | [[Category: Verdine, G L.]] | ||
- | [[Category: GOL]] | ||
[[Category: alka]] | [[Category: alka]] | ||
[[Category: base excision]] | [[Category: base excision]] | ||
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[[Category: methylation]] | [[Category: methylation]] | ||
- | ''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 22:19:21 2008'' |
Revision as of 19:19, 30 March 2008
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, resolution 1.80Å | |||||||
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Ligands: | |||||||
Gene: | ALKA (Escherichia coli) | ||||||
Activity: | DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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 Sun Mar 30 22:19:21 2008