1m3q

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(New page: 200px<br /> <applet load="1m3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3q, resolution 1.90&Aring;" /> '''Crystal Structure o...)
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<applet load="1m3q" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1m3q, resolution 1.90&Aring;" />
'''Crystal Structure of hogg1 D268E Mutant with Base-Excised DNA and 8-aminoguanine'''<br />
'''Crystal Structure of hogg1 D268E Mutant with Base-Excised DNA and 8-aminoguanine'''<br />
==Overview==
==Overview==
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DNA glycosylase/lyases initiate the repair of damaged nucleobases in the, genome by catalyzing excision of aberrant nucleobases and nicking of the, lesion-containing DNA strand. Nearly all of these proteins have the, unusual property of remaining tightly bound in vitro to the end products, of the reaction cascade. We have taken advantage of this property to, crystallize and structurally characterize the end product resulting from, complete DNA processing by a catalytically active mutant form of human, 8-oxoguanine DNA glycosylase (D268E hOgg1). The resulting structure is, consistent with the currently accepted catalytic mechanism for the, protein. Unexpectedly, however, soaking of a nucleobase analog into the, crystals results in religation of the DNA backbone in situ.
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DNA glycosylase/lyases initiate the repair of damaged nucleobases in the genome by catalyzing excision of aberrant nucleobases and nicking of the lesion-containing DNA strand. Nearly all of these proteins have the unusual property of remaining tightly bound in vitro to the end products of the reaction cascade. We have taken advantage of this property to crystallize and structurally characterize the end product resulting from complete DNA processing by a catalytically active mutant form of human 8-oxoguanine DNA glycosylase (D268E hOgg1). The resulting structure is consistent with the currently accepted catalytic mechanism for the protein. Unexpectedly, however, soaking of a nucleobase analog into the crystals results in religation of the DNA backbone in situ.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1M3Q 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=1M3Q OCA].
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1M3Q 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=1M3Q OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chung, S.J.]]
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[[Category: Chung, S J.]]
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[[Category: Verdine, G.L.]]
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[[Category: Verdine, G L.]]
[[Category: ANG]]
[[Category: ANG]]
[[Category: CA]]
[[Category: CA]]
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[[Category: re-ligation]]
[[Category: re-ligation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:06:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:06 2008''

Revision as of 11:51, 21 February 2008

Image:1m3q.gif

1m3q, resolution 1.90Å

Drag the structure with the mouse to rotate

Crystal Structure of hogg1 D268E Mutant with Base-Excised DNA and 8-aminoguanine

Contents

Overview

DNA glycosylase/lyases initiate the repair of damaged nucleobases in the genome by catalyzing excision of aberrant nucleobases and nicking of the lesion-containing DNA strand. Nearly all of these proteins have the unusual property of remaining tightly bound in vitro to the end products of the reaction cascade. We have taken advantage of this property to crystallize and structurally characterize the end product resulting from complete DNA processing by a catalytically active mutant form of human 8-oxoguanine DNA glycosylase (D268E hOgg1). The resulting structure is consistent with the currently accepted catalytic mechanism for the protein. Unexpectedly, however, soaking of a nucleobase analog into the crystals results in religation of the DNA backbone in situ.

Disease

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

About this Structure

1M3Q is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structures of end products resulting from lesion processing by a DNA glycosylase/lyase., Chung SJ, Verdine GL, Chem Biol. 2004 Dec;11(12):1643-9. PMID:15610848

Page seeded by OCA on Thu Feb 21 13:51:06 2008

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