4od8: Difference between revisions

Line 1:

~~'''Unreleased~~ structure~~'''~~

===Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus===

~~The entry 4od8 is ON HOLD~~

==Function==

[[http://www.uniprot.org/uniprot/UNG_VACCC UNG_VACCC]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity). [[http://www.uniprot.org/uniprot/A20_VACCC A20_VACCC]] Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity).

~~Authors~~: ~~Contesto-Richefeu, C~~.~~, Tarbouriech, N~~.~~, Brazzolotto, X~~.~~, Burmeister, W.P., Iseni, F~~.

==About this Structure==

[[4od8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OD8 OCA].

~~Description~~: ~~Crystal structure of the vaccinia virus~~ DNA polymerase ~~holoenzyme subunit D4 in~~ complex ~~with the A20 N-terminus~~

==Reference==

[[Category: Uracil-DNA glycosylase]]

[[Category: Brazzolotto, X.]]

[[Category: Burmeister, W P.]]

[[Category: Contesto-Richefeu, C.]]

[[Category: Iseni, F.]]

[[Category: Tarbouriech, N.]]

[[Category: Dna binding]]

[[Category: Dna polymerase binding]]

[[Category: Dna polymerase processivity factor]]

[[Category: Hydrolase-replication complex]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4od8|  PDB=4od8  |  SCENE=  }}
+===Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus===
+{{ABSTRACT_PUBMED_24603707}}
-The entry 4od8 is ON HOLD
+==Function==
+[[http://www.uniprot.org/uniprot/UNG_VACCC UNG_VACCC]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity). [[http://www.uniprot.org/uniprot/A20_VACCC A20_VACCC]] Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity).
-Authors: Contesto-Richefeu, C., Tarbouriech, N., Brazzolotto, X., Burmeister, W.P., Iseni, F.
+==About this Structure==
+[[4od8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OD8 OCA].
-Description: Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus
+==Reference==
+<ref group="xtra">PMID:024603707</ref><references group="xtra"/><references/>
+[[Category: Uracil-DNA glycosylase]]
+[[Category: Brazzolotto, X.]]
+[[Category: Burmeister, W P.]]
+[[Category: Contesto-Richefeu, C.]]
+[[Category: Iseni, F.]]
+[[Category: Tarbouriech, N.]]
+[[Category: Dna binding]]
+[[Category: Dna polymerase binding]]
+[[Category: Dna polymerase processivity factor]]
+[[Category: Hydrolase-replication complex]]