1p7m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p7m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1p7m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p7m| PDB=1p7m | SCENE= }}
{{STRUCTURE_1p7m| PDB=1p7m | SCENE= }}
-
'''SOLUTION STRUCTURE AND BASE PERTURBATION STUDIES REVEAL A NOVEL MODE OF ALKYLATED BASE RECOGNITION BY 3-METHYLADENINE DNA GLYCOSYLASE I'''
+
===SOLUTION STRUCTURE AND BASE PERTURBATION STUDIES REVEAL A NOVEL MODE OF ALKYLATED BASE RECOGNITION BY 3-METHYLADENINE DNA GLYCOSYLASE I===
-
==Overview==
+
<!--
-
The specific recognition mechanisms of DNA repair glycosylases that remove cationic alkylpurine bases in DNA are not well understood partly due to the absence of structures of these enzymes with their cognate bases. Here we report the solution structure of 3-methyladenine DNA glycosylase I (TAG) in complex with its 3-methyladenine (3-MeA) cognate base, and we have used chemical perturbation of the base in combination with mutagenesis of the enzyme to evaluate the role of hydrogen bonding and pi-cation interactions in alkylated base recognition by this DNA repair enzyme. We find that TAG uses hydrogen bonding with heteroatoms on the base, van der Waals interactions with the 3-Me group, and conventional pi-pi stacking with a conserved Trp side chain to selectively bind neutral 3-MeA over the cationic form of the base. Discrimination against binding of the normal base adenine is derived from direct sensing of the 3-methyl group, leading to an induced-fit conformational change that engulfs the base in a box defined by five aromatic side chains. These findings indicate that base specific recognition by TAG does not involve strong pi-cation interactions, and suggest a novel mechanism for alkylated base recognition and removal.
+
The line below this paragraph, {{ABSTRACT_PUBMED_13129925}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 13129925 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_13129925}}
==About this Structure==
==About this Structure==
-
1P7M 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=1P7M OCA].
+
1P7M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P7M OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Stivers, J T.]]
[[Category: Stivers, J T.]]
[[Category: 3-methyladenine tag complex nmr]]
[[Category: 3-methyladenine tag complex nmr]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:47:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:13:57 2008''

Revision as of 02:14, 28 July 2008

Image:1p7m.png

Template:STRUCTURE 1p7m

SOLUTION STRUCTURE AND BASE PERTURBATION STUDIES REVEAL A NOVEL MODE OF ALKYLATED BASE RECOGNITION BY 3-METHYLADENINE DNA GLYCOSYLASE I

Template:ABSTRACT PUBMED 13129925

About this Structure

1P7M is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Solution structure and base perturbation studies reveal a novel mode of alkylated base recognition by 3-methyladenine DNA glycosylase I., Cao C, Kwon K, Jiang YL, Drohat AC, Stivers JT, J Biol Chem. 2003 Nov 28;278(48):48012-20. Epub 2003 Sep 16. PMID:13129925

Page seeded by OCA on Mon Jul 28 05:13:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p7m"
Personal tools