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1weg

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{{STRUCTURE_1weg| PDB=1weg | SCENE= }}
{{STRUCTURE_1weg| PDB=1weg | SCENE= }}
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'''Catalytic Domain Od Muty Form Escherichia Coli K142A Mutant'''
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===Catalytic Domain Od Muty Form Escherichia Coli K142A Mutant===
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==Overview==
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The Escherichia coli adenine DNA glycosylase, MutY, plays an important role in the maintenance of genomic stability by catalyzing the removal of adenine opposite 8-oxo-7,8-dihydroguanine or guanine in duplex DNA. Although the x-ray crystal structure of the catalytic domain of MutY revealed a mechanism for catalysis of the glycosyl bond, it appeared that several opportunistically positioned lysine side chains could participate in a secondary beta-elimination reaction. In this investigation, it is established via site-directed mutagenesis and the determination of a 1.35-A structure of MutY in complex with adenine that the abasic site (apurinic/apyrimidinic) lyase activity is alternatively regulated by two lysines, Lys142 and Lys20. Analyses of the crystallographic structure also suggest a role for Glu161 in the apurinic/apyrimidinic lyase chemistry. The beta-elimination reaction is structurally and chemically uncoupled from the initial glycosyl bond scission, indicating that this reaction occurs as a consequence of active site plasticity and slow dissociation of the product complex. MutY with either the K142A or K20A mutation still catalyzes beta and beta-delta elimination reactions, and both mutants can be trapped as covalent enzyme-DNA intermediates by chemical reduction. The trapping was observed to occur both pre- and post-phosphodiester bond scission, establishing that both of these intermediates have significant half-lives. Thus, the final spectrum of DNA products generated reflects the outcome of a delicate balance of closely related equilibrium constants.
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(as it appears on PubMed at http://www.pubmed.gov), where 15326180 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15326180}}
==About this Structure==
==About this Structure==
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[[Category: Tainer, J A.]]
[[Category: Tainer, J A.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:32:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:36:24 2008''

Revision as of 15:36, 28 July 2008

Image:1weg.jpg

Template:STRUCTURE 1weg

Catalytic Domain Od Muty Form Escherichia Coli K142A Mutant

Template:ABSTRACT PUBMED 15326180

About this Structure

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

Reference

Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase., Manuel RC, Hitomi K, Arvai AS, House PG, Kurtz AJ, Dodson ML, McCullough AK, Tainer JA, Lloyd RS, J Biol Chem. 2004 Nov 5;279(45):46930-9. Epub 2004 Aug 23. PMID:15326180

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