4l5n: Difference between revisions

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'''Unreleased structure'''


The entry 4l5n is ON HOLD
==Crystallographic Structure of HHV-1 Uracil-DNA Glycosylase complexed with the Bacillus phage PZA inhibitor protein p56==
<StructureSection load='4l5n' size='340' side='right'caption='[[4l5n]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4l5n]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_PZA Bacillus phage PZA] and [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L5N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4l5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l5n OCA], [https://pdbe.org/4l5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l5n RCSB], [https://www.ebi.ac.uk/pdbsum/4l5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l5n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UNG_HHV11 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.<ref>PMID:7552746</ref> <ref>PMID:16306042</ref>


Authors: Cole, A.R., Sapir, O., Ryzhenkova, K., Baltulionis, G., Hornyak, P., Savva, R.
==See Also==
 
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
Description: Crystallographic Structure of HHV1 Uracil DNA Glycosylase bound to the p56 inhibitor
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus phage PZA]]
[[Category: Human alphaherpesvirus 1 strain 17]]
[[Category: Large Structures]]
[[Category: Baltulionis G]]
[[Category: Cole AR]]
[[Category: Hornyak P]]
[[Category: Ryzhenkova K]]
[[Category: Sapir O]]
[[Category: Savva R]]

Latest revision as of 15:17, 1 March 2024

Crystallographic Structure of HHV-1 Uracil-DNA Glycosylase complexed with the Bacillus phage PZA inhibitor protein p56Crystallographic Structure of HHV-1 Uracil-DNA Glycosylase complexed with the Bacillus phage PZA inhibitor protein p56

Structural highlights

4l5n is a 6 chain structure with sequence from Bacillus phage PZA and Human alphaherpesvirus 1 strain 17. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.16Å
Ligands:
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]

See Also

References

  1. ↑ 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
  2. ↑ 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

4l5n, resolution 2.16Å

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