5yd8: Difference between revisions

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'''Unreleased structure'''


The entry 5yd8 is ON HOLD until Paper Publication
==Crystal structure of human PCNA in complex with APIM of human ZRANB3==
 
<StructureSection load='5yd8' size='340' side='right' caption='[[5yd8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5yd8]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YD8 FirstGlance]. <br>
Description:  
</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=5yd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yd8 OCA], [http://pdbe.org/5yd8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yd8 RCSB], [http://www.ebi.ac.uk/pdbsum/5yd8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yd8 ProSAT]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PCNA_HUMAN PCNA_HUMAN]] Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.<ref>PMID:19443450</ref> <ref>PMID:18719106</ref>  [[http://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN]] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hashimoto, H]]
[[Category: Tagata, R]]
[[Category: Complex]]
[[Category: Dna binding protein]]

Revision as of 08:41, 18 April 2018

Crystal structure of human PCNA in complex with APIM of human ZRANB3Crystal structure of human PCNA in complex with APIM of human ZRANB3

Structural highlights

5yd8 is a 6 chain structure. 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

[PCNA_HUMAN] Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.[1] [2] [ZRAB3_HUMAN] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.[3] [4] [5] [6] [7]

References

  1. ↑ Burkovics P, Hajdu I, Szukacsov V, Unk I, Haracska L. Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage. Nucleic Acids Res. 2009 Jul;37(13):4247-55. doi: 10.1093/nar/gkp357. Epub 2009, May 13. PMID:19443450 doi:10.1093/nar/gkp357
  2. ↑ Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung K. Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks. Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12411-6. Epub 2008 Aug 21. PMID:18719106 doi:0805685105
  3. ↑ Yusufzai T, Kadonaga JT. Annealing helicase 2 (AH2), a DNA-rewinding motor with an HNH motif. Proc Natl Acad Sci U S A. 2010 Dec 7;107(49):20970-3. Epub 2010 Nov 15. PMID:21078962 doi:10.1073/pnas.1011196107
  4. ↑ Ciccia A, Nimonkar AV, Hu Y, Hajdu I, Achar YJ, Izhar L, Petit SA, Adamson B, Yoon JC, Kowalczykowski SC, Livingston DM, Haracska L, Elledge SJ. Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic integrity after replication stress. Mol Cell. 2012 Aug 10;47(3):396-409. doi: 10.1016/j.molcel.2012.05.024. Epub 2012, Jun 14. PMID:22704558 doi:http://dx.doi.org/10.1016/j.molcel.2012.05.024
  5. ↑ Yuan J, Ghosal G, Chen J. The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and participates in cellular response to replication stress. Mol Cell. 2012 Aug 10;47(3):410-21. doi: 10.1016/j.molcel.2012.05.025. Epub 2012 , Jun 14. PMID:22705370 doi:http://dx.doi.org/10.1016/j.molcel.2012.05.025
  6. ↑ Weston R, Peeters H, Ahel D. ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress response. Genes Dev. 2012 Jul 15;26(14):1558-72. doi: 10.1101/gad.193516.112. Epub 2012 Jul, 3. PMID:22759634 doi:http://dx.doi.org/10.1101/gad.193516.112
  7. ↑ Badu-Nkansah A, Mason AC, Eichman BF, Cortez D. Identification of a Substrate Recognition Domain in the Replication Stress Response Protein Zinc Finger Ran-binding Domain-containing Protein 3 (ZRANB3). J Biol Chem. 2016 Apr 8;291(15):8251-7. doi: 10.1074/jbc.M115.709733. Epub 2016, Feb 16. PMID:26884333 doi:http://dx.doi.org/10.1074/jbc.M115.709733

5yd8, resolution 2.30Å

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