1lau

From Proteopedia

(Difference between revisions)

Revision as of 07:50, 4 November 2020

URACIL-DNA GLYCOSYLASE

Structural highlights

1lau is a 2 chain structure with sequence from Human herpesvirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UNG_HHV11] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly, in terminally differentiated neurons which lack DNA repair enzymes.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision.

The structural basis of specific base-excision repair by uracil-DNA glycosylase.,Savva R, McAuley-Hecht K, Brown T, Pearl L Nature. 1995 Feb 9;373(6514):487-93. PMID:7845459^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Savva R, Pearl LH. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. Nat Struct Biol. 1995 Sep;2(9):752-7. PMID:7552746
↑ Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS. A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1. J Biol Chem. 2006 Feb 24;281(8):4983-92. Epub 2005 Nov 22. PMID:16306042 doi:http://dx.doi.org/10.1074/jbc.M509137200
↑ Savva R, McAuley-Hecht K, Brown T, Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature. 1995 Feb 9;373(6514):487-93. PMID:7845459 doi:http://dx.doi.org/10.1038/373487a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lau"

@@ Line 1: / Line 1: @@
 ==URACIL-DNA GLYCOSYLASE==
-<StructureSection load='1lau' size='340' side='right' caption='[[1lau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1lau' size='340' side='right'caption='[[1lau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lau]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lau]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LAU FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lau OCA], [http://pdbe.org/1lau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lau RCSB], [http://www.ebi.ac.uk/pdbsum/1lau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lau ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lau OCA], [http://pdbe.org/1lau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lau RCSB], [http://www.ebi.ac.uk/pdbsum/1lau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lau ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[DNA glycosylase|DNA glycosylase]]
+*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Human herpesvirus 1]]
+[[Category: Large Structures]]
 [[Category: Pearl, L H]]
 [[Category: Savva, R]]

1lau

From Proteopedia

Revision as of 07:50, 4 November 2020

URACIL-DNA GLYCOSYLASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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