1m3h: Difference between revisions
New page: left|200px<br /> <applet load="1m3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3h, resolution 2.05Å" /> '''Crystal Structure o... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1m3h.gif|left|200px]]<br /> | [[Image:1m3h.gif|left|200px]]<br /><applet load="1m3h" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1m3h" size=" | |||
caption="1m3h, resolution 2.05Å" /> | caption="1m3h, resolution 2.05Å" /> | ||
'''Crystal Structure of Hogg1 D268E Mutant with Product Oligonucleotide'''<br /> | '''Crystal Structure of Hogg1 D268E Mutant with Product Oligonucleotide'''<br /> | ||
==Overview== | ==Overview== | ||
DNA glycosylase/lyases initiate the repair of damaged nucleobases in the | 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== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1M3H 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1M3H 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3H OCA]. | ||
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chung, S | [[Category: Chung, S J.]] | ||
[[Category: Verdine, G | [[Category: Verdine, G L.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: dna glycosylase]] | [[Category: dna glycosylase]] | ||
| Line 27: | Line 26: | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:06 2008'' | ||
Revision as of 14:51, 21 February 2008
|
Crystal Structure of Hogg1 D268E Mutant with Product Oligonucleotide
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]
About this StructureAbout this Structure
1M3H is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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