1pu6: Difference between revisions

Revision as of 00:13, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pu6.png

Template:STRUCTURE 1pu6

Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII)Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII)

Template:ABSTRACT PUBMED 14517230

About this StructureAbout this Structure

1PU6 is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases., Eichman BF, O'Rourke EJ, Radicella JP, Ellenberger T, EMBO J. 2003 Oct 1;22(19):4898-909. PMID:14517230

Page seeded by OCA on Mon Jul 28 00:13:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1pu6.gif|left|200px]]
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 {{STRUCTURE_1pu6|  PDB=1pu6  |  SCENE=  }}
-'''Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII)'''
+===Crystal structure of H.pylori 3-methyladenine DNA glycosylase (MagIII)===
-==Overview==
+<!--
-DNA glycosylases catalyze the excision of chemically modified bases from DNA. Although most glycosylases are specific to a particular base, the 3-methyladenine (m3A) DNA glycosylases include both highly specific enzymes acting on a single modified base, and enzymes with broader specificity for alkylation-damaged DNA. Our structural understanding of these different enzymatic specificities is currently limited to crystal and NMR structures of the unliganded enzymes and complexes with abasic DNA inhibitors. Presented here are high-resolution crystal structures of the m3A DNA glycosylase from Helicobacter pylori (MagIII) in the unliganded form and bound to alkylated bases 3,9-dimethyladenine and 1,N6-ethenoadenine. These are the first structures of a nucleobase bound in the active site of a m3A glycosylase belonging to the helix-hairpin-helix superfamily. MagIII achieves its specificity for positively-charged m3A not by direct interactions with purine or methyl substituent atoms, but rather by stacking the base between two aromatic side chains in a pocket that excludes 7-methylguanine. We report base excision and DNA binding activities of MagIII active site mutants, together with a structural comparison of the HhH glycosylases.
+The line below this paragraph, {{ABSTRACT_PUBMED_14517230}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14517230 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14517230}}
 ==About this Structure==
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 [[Category: Glycosylase]]
 [[Category: Helix-hairpin-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:29:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:13:42 2008''