4l60: Difference between revisions
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==Structure of C81R Mutant PCNA Protein Defective in Mismatch Repair== | ==Structure of C81R Mutant PCNA Protein Defective in Mismatch Repair== | ||
<StructureSection load='4l60' size='340' side='right' caption='[[4l60]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4l60' size='340' side='right'caption='[[4l60]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4l60]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L60 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4l60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L60 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.003Å</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=4l60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l60 OCA], [https://pdbe.org/4l60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l60 RCSB], [https://www.ebi.ac.uk/pdbsum/4l60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l60 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[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> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4l60" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Proliferating | *[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Boehm E]] | ||
[[Category: | [[Category: Washington T]] | ||
Latest revision as of 19:12, 20 September 2023
Structure of C81R Mutant PCNA Protein Defective in Mismatch RepairStructure of C81R Mutant PCNA Protein Defective in Mismatch Repair
Structural highlights
FunctionPCNA_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.[1] [2] Publication Abstract from PubMedDuring DNA replication, mismatches and small loops in the DNA resulting from insertions or deletions are repaired by the mismatch repair (MMR) machinery. Proliferating cell nuclear antigen (PCNA) plays an important role in both mismatch-recognition and resynthesis stages of MMR. Previously, two mutant forms of PCNA were identified that cause defects in MMR with little, if any, other defects. The C22Y mutant PCNA protein completely blocks MutSalpha-dependent MMR, and the C81R mutant PCNA protein partially blocks both MutSalpha-dependent and MutSbeta-dependent MMR. In order to understand the structural and mechanistic basis by which these two amino acid substitutions in PCNA proteins block MMR, we solved the X-ray crystal structures of both mutant proteins and carried out further biochemical studies. We found that these amino acid substitutions lead to subtle, distinct structural changes in PCNA. The C22Y substitution alters the positions of the alpha-helices lining the central hole of the PCNA ring, whereas the C81R substitution creates a distortion in an extended loop near the PCNA subunit interface. We conclude that the structural integrity of the alpha-helices lining the central hole and this loop are both necessary to form productive complexes with MutSalpha and mismatch-containing DNA. Distinct structural alterations in proliferating cell nuclear antigen block DNA mismatch repair.,Dieckman LM, Boehm EM, Hingorani MM, Washington MT Biochemistry. 2013 Aug 20;52(33):5611-9. doi: 10.1021/bi400378e. Epub 2013 Aug 2. PMID:23869605[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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