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1lwy

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(New page: 200px<br /> <applet load="1lwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lwy, resolution 2.01&Aring;" /> '''hOgg1 Borohydride-T...)
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'''hOgg1 Borohydride-Trapped Intermediate without 8-oxoguanine'''<br />
'''hOgg1 Borohydride-Trapped Intermediate without 8-oxoguanine'''<br />
==Overview==
==Overview==
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Most spontaneous damage to bases in DNA is corrected through the action of, the base-excision DNA repair pathway. Base excision repair is initiated by, DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in, DNA and catalyze their excision. How such proteins accomplish the feat of, catalyzing no fewer than five sequential reaction steps using a single, active site has been unknown. To help answer this, we report the structure, of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine, DNA glycosylase. This structure and supporting biochemical results reveal, that the enzyme sequesters the excised lesion base and exploits it as a, cofactor to participate in catalysis. To our knowledge, the present, example represents the first documented case of product-assisted catalysis, in an enzyme-catalyzed reaction.
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Most spontaneous damage to bases in DNA is corrected through the action of the base-excision DNA repair pathway. Base excision repair is initiated by DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in DNA and catalyze their excision. How such proteins accomplish the feat of catalyzing no fewer than five sequential reaction steps using a single active site has been unknown. To help answer this, we report the structure of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine DNA glycosylase. This structure and supporting biochemical results reveal that the enzyme sequesters the excised lesion base and exploits it as a cofactor to participate in catalysis. To our knowledge, the present example represents the first documented case of product-assisted catalysis in an enzyme-catalyzed reaction.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1LWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LWY OCA].
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1LWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWY OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bruner, S.D.]]
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[[Category: Bruner, S D.]]
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[[Category: Fromme, J.C.]]
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[[Category: Fromme, J C.]]
[[Category: Karplus, M.]]
[[Category: Karplus, M.]]
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[[Category: Verdine, G.L.]]
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[[Category: Verdine, G L.]]
[[Category: Yang, W.]]
[[Category: Yang, W.]]
[[Category: borohydride]]
[[Category: borohydride]]
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[[Category: reaction intermediate]]
[[Category: reaction intermediate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:04:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:16 2008''

Revision as of 11:49, 21 February 2008

Image:1lwy.gif

1lwy, resolution 2.01Å

Drag the structure with the mouse to rotate

hOgg1 Borohydride-Trapped Intermediate without 8-oxoguanine

Contents

Overview

Most spontaneous damage to bases in DNA is corrected through the action of the base-excision DNA repair pathway. Base excision repair is initiated by DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in DNA and catalyze their excision. How such proteins accomplish the feat of catalyzing no fewer than five sequential reaction steps using a single active site has been unknown. To help answer this, we report the structure of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine DNA glycosylase. This structure and supporting biochemical results reveal that the enzyme sequesters the excised lesion base and exploits it as a cofactor to participate in catalysis. To our knowledge, the present example represents the first documented case of product-assisted catalysis in an enzyme-catalyzed reaction.

Disease

Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]

About this Structure

1LWY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Product-assisted catalysis in base-excision DNA repair., Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL, Nat Struct Biol. 2003 Mar;10(3):204-11. PMID:12592398

Page seeded by OCA on Thu Feb 21 13:49:16 2008

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