1akz: Difference between revisions
New page: left|200px<br /> <applet load="1akz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1akz, resolution 1.57Å" /> '''HUMAN URACIL-DNA GL... |
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[[Image:1akz.gif|left|200px]]<br /> | [[Image:1akz.gif|left|200px]]<br /><applet load="1akz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''HUMAN URACIL-DNA GLYCOSYLASE'''<br /> | '''HUMAN URACIL-DNA GLYCOSYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
Crystal structures of the DNA repair enzyme human uracil-DNA glycosylase | Crystal structures of the DNA repair enzyme human uracil-DNA glycosylase (UDG), combined with mutational analysis, reveal the structural basis for the specificity of the enzyme. Within the classic alpha/beta fold of UDG, sequence-conserved residues form a positively charged, active-site groove the width of duplex DNA, at the C-terminal edge of the central four-stranded parallel beta sheet. In the UDG-6-aminouracil complex, uracil binds at the base of the groove within a rigid preformed pocket that confers selectivity for uracil over other bases by shape complementary and by main chain and Asn-204 side chain hydrogen bonds. Main chain nitrogen atoms are positioned to stabilize the oxyanion intermediate generated by His-268 acting via nucleophilic attack or general base mechanisms. Specific binding of uracil flipped out from a DNA duplex provides a structural mechanism for damaged base recognition. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1AKZ 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:// | 1AKZ 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=1AKZ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tainer, C | [[Category: Tainer, C D.M J.A.]] | ||
[[Category: alpha/ beta protein]] | [[Category: alpha/ beta protein]] | ||
[[Category: dna repair]] | [[Category: dna repair]] | ||
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[[Category: uracil removal from dna]] | [[Category: uracil removal from dna]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:43 2008'' | ||
Revision as of 12:45, 21 February 2008
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HUMAN URACIL-DNA GLYCOSYLASE
OverviewOverview
Crystal structures of the DNA repair enzyme human uracil-DNA glycosylase (UDG), combined with mutational analysis, reveal the structural basis for the specificity of the enzyme. Within the classic alpha/beta fold of UDG, sequence-conserved residues form a positively charged, active-site groove the width of duplex DNA, at the C-terminal edge of the central four-stranded parallel beta sheet. In the UDG-6-aminouracil complex, uracil binds at the base of the groove within a rigid preformed pocket that confers selectivity for uracil over other bases by shape complementary and by main chain and Asn-204 side chain hydrogen bonds. Main chain nitrogen atoms are positioned to stabilize the oxyanion intermediate generated by His-268 acting via nucleophilic attack or general base mechanisms. Specific binding of uracil flipped out from a DNA duplex provides a structural mechanism for damaged base recognition.
DiseaseDisease
Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[191525]
About this StructureAbout this Structure
1AKZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis., Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA, Cell. 1995 Mar 24;80(6):869-78. PMID:7697717
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