1lwv: Difference between revisions

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New page: left|200px<br /> <applet load="1lwv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lwv, resolution 2.3Å" /> '''Borohydride-trapped ...
 
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[[Image:1lwv.gif|left|200px]]<br />
[[Image:1lwv.gif|left|200px]]<br /><applet load="1lwv" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1lwv" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1lwv, resolution 2.3&Aring;" />
caption="1lwv, resolution 2.3&Aring;" />
'''Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-aminoguanine'''<br />
'''Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-aminoguanine'''<br />


==Overview==
==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.
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==
1LWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and ANG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LWV OCA].  
1LWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ANG:'>ANG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWV OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bruner, S.D.]]
[[Category: Bruner, S D.]]
[[Category: Fromme, J.C.]]
[[Category: Fromme, J C.]]
[[Category: Karplus, M.]]
[[Category: Karplus, M.]]
[[Category: Verdine, G.L.]]
[[Category: Verdine, G L.]]
[[Category: Yang, W.]]
[[Category: Yang, W.]]
[[Category: ANG]]
[[Category: ANG]]
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[[Category: reaction intermediate]]
[[Category: reaction intermediate]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:04:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:17 2008''