1akz

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[[Image:1akz.gif|left|200px]]<br /><applet load="1akz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1akz.gif|left|200px]]
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caption="1akz, resolution 1.57&Aring;" />
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'''HUMAN URACIL-DNA GLYCOSYLASE'''<br />
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{{Structure
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|PDB= 1akz |SIZE=350|CAPTION= <scene name='initialview01'>1akz</scene>, resolution 1.57&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''HUMAN URACIL-DNA GLYCOSYLASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1AKZ is a [[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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7697717 7697717]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7697717 7697717]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: uracil removal from dna]]
[[Category: uracil removal from dna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:01 2008''

Revision as of 07:59, 20 March 2008

Image:1akz.gif


PDB ID 1akz

Drag the structure with the mouse to rotate
, resolution 1.57Å
Coordinates: save as pdb, mmCIF, xml



HUMAN URACIL-DNA GLYCOSYLASE


Contents

Overview

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

Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[191525]

About this Structure

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

Reference

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

Page seeded by OCA on Thu Mar 20 09:59:01 2008

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