1mud: Difference between revisions

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[[Image:1mud.~~gif~~|left|200px]]

[[Image:1mud.png|left|200px]]

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~~'''~~CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI, D138N MUTANT COMPLEXED TO ADENINE~~'''~~

===CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI, D138N MUTANT COMPLEXED TO ADENINE===

~~==Overview==~~

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The ~~DNA glycosylase MutY~~, ~~which is a member of~~ the ~~Helix-hairpin-Helix~~ (~~HhH) DNA glycosylase superfamily, excises adenine from mispairs with 8-oxoguanine and guanine~~. ~~High-resolution crystal structures of the MutY catalytic core (cMutY~~), the ~~complex with bound adenine, and designed mutants reveal the basis for adenine specificity and glycosyl bond cleavage chemistry~~. ~~The two cMutY helical domains form a positively~~-~~charged groove with the adenine~~-specific pocket at their interface. The Watson-Crick hydrogen bond partners of the bound adenine are substituted by protein atoms, confirming a nucleotide flipping mechanism, and supporting a specific DNA binding orientation by MutY and structurally related DNA glycosylases.

The line below this paragraph, {{ABSTRACT_PUBMED_9846876}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9846876 is the PubMed ID number.

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==About this Structure==

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[[Category: Dna g a mismatch repair enzyme]]

[[Category: Dna repair]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 01~~:43:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:32:48 2008''

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-[[Image:1mud.gif|left|200px]]
+{{Seed}}
+[[Image:1mud.png|left|200px]]
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 {{STRUCTURE_1mud|  PDB=1mud  |  SCENE=  }}
-'''CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI, D138N MUTANT COMPLEXED TO ADENINE'''
+===CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI, D138N MUTANT COMPLEXED TO ADENINE===
-==Overview==
+<!--
-The DNA glycosylase MutY, which is a member of the Helix-hairpin-Helix (HhH) DNA glycosylase superfamily, excises adenine from mispairs with 8-oxoguanine and guanine. High-resolution crystal structures of the MutY catalytic core (cMutY), the complex with bound adenine, and designed mutants reveal the basis for adenine specificity and glycosyl bond cleavage chemistry. The two cMutY helical domains form a positively-charged groove with the adenine-specific pocket at their interface. The Watson-Crick hydrogen bond partners of the bound adenine are substituted by protein atoms, confirming a nucleotide flipping mechanism, and supporting a specific DNA binding orientation by MutY and structurally related DNA glycosylases.
+The line below this paragraph, {{ABSTRACT_PUBMED_9846876}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9846876 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9846876}}
 ==About this Structure==
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 [[Category: Dna g a mismatch repair enzyme]]
 [[Category: Dna repair]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:43:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:32:48 2008''