1plr

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<StructureSection load='1plr' size='340' side='right'caption='[[1plr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1plr' size='340' side='right'caption='[[1plr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1plr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1plr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLR FirstGlance]. <br>
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</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=1plr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plr OCA], [https://pdbe.org/1plr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plr RCSB], [https://www.ebi.ac.uk/pdbsum/1plr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plr ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1plr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plr OCA], [https://pdbe.org/1plr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plr RCSB], [https://www.ebi.ac.uk/pdbsum/1plr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST]] This protein is an 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. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref>
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[https://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST] This protein is an 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. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1plr ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1plr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of the processivity factor required by eukaryotic DNA polymerase delta, proliferating cell nuclear antigen (PCNA) from S. cerevisiae, has been determined at 2.3 A resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly associated to form a closed ring. The dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is strikingly similar to the dimeric ring formed by the beta subunit (processivity factor) of E. coli DNA polymerase III holoenzyme, with which it shares no significant sequence identity. This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds.
 
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Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA.,Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J Cell. 1994 Dec 30;79(7):1233-43. PMID:8001157<ref>PMID:8001157</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1plr" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Enkephalin 3D structures|Enkephalin 3D structures]]
*[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]]
*[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Burgers, P M]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Gary, S]]
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[[Category: Burgers PM]]
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[[Category: Kong, X P]]
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[[Category: Gary S]]
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[[Category: Krishna, T S.R]]
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[[Category: Kong X-P]]
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[[Category: Kuriyan, J]]
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[[Category: Krishna TSR]]
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[[Category: Dna replication]]
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[[Category: Kuriyan J]]
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[[Category: Dna-binding]]
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[[Category: Nuclear protein]]
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Revision as of 05:56, 17 April 2024

CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA

PDB ID 1plr

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