1weg

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[[Image:1weg.jpg|left|200px]]<br /><applet load="1weg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1weg.jpg|left|200px]]
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caption="1weg, resolution 1.80&Aring;" />
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'''Catalytic Domain Od Muty Form Escherichia Coli K142A Mutant'''<br />
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{{Structure
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|PDB= 1weg |SIZE=350|CAPTION= <scene name='initialview01'>1weg</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene> and <scene name='pdbligand=SF4:IRON/SULFUR CLUSTER'>SF4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Catalytic Domain Od Muty Form Escherichia Coli K142A Mutant'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1WEG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=EDO:'>EDO</scene>, <scene name='pdbligand=IMD:'>IMD</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WEG OCA].
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1WEG 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=1WEG OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15326180 15326180]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15326180 15326180]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:43:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:55:56 2008''

Revision as of 12:55, 20 March 2008

Image:1weg.jpg


PDB ID 1weg

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Catalytic Domain Od Muty Form Escherichia Coli K142A Mutant


Overview

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.

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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