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1mun

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{{STRUCTURE_1mun| PDB=1mun | SCENE= }}
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'''CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT'''
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===CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9846876 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9846876}}
==About this Structure==
==About this Structure==
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:24:01 2008''

Revision as of 09:24, 27 July 2008

Image:1mun.png

Template:STRUCTURE 1mun

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT

Template:ABSTRACT PUBMED 9846876

About this Structure

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

Reference

MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily., Guan Y, Manuel RC, Arvai AS, Parikh SS, Mol CD, Miller JH, Lloyd S, Tainer JA, Nat Struct Biol. 1998 Dec;5(12):1058-64. PMID:9846876

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