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4od8

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'''Unreleased structure'''
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{{STRUCTURE_4od8| PDB=4od8 | SCENE= }}
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===Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus===
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{{ABSTRACT_PUBMED_24603707}}
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The entry 4od8 is ON HOLD
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==Function==
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[[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).
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Authors: Contesto-Richefeu, C., Tarbouriech, N., Brazzolotto, X., Burmeister, W.P., Iseni, F.
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==About this Structure==
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[[4od8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OD8 OCA].
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Description: Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus
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==Reference==
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<ref group="xtra">PMID:024603707</ref><references group="xtra"/><references/>
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[[Category: Uracil-DNA glycosylase]]
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[[Category: Brazzolotto, X.]]
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[[Category: Burmeister, W P.]]
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[[Category: Contesto-Richefeu, C.]]
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[[Category: Iseni, F.]]
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[[Category: Tarbouriech, N.]]
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[[Category: Dna binding]]
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[[Category: Dna polymerase binding]]
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[[Category: Dna polymerase processivity factor]]
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[[Category: Hydrolase-replication complex]]

Revision as of 09:23, 26 March 2014

Template:STRUCTURE 4od8

Contents

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

Template:ABSTRACT PUBMED 24603707

Function

[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). [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).

About this Structure

4od8 is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Contesto-Richefeu C, Tarbouriech N, Brazzolotto X, Betzi S, Morelli X, Burmeister WP, Iseni F. Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit d4 in complex with the a20 N-terminal domain. PLoS Pathog. 2014 Mar 6;10(3):e1003978. doi: 10.1371/journal.ppat.1003978., eCollection 2014 Mar. PMID:24603707 doi:http://dx.doi.org/10.1371/journal.ppat.1003978

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