4xvm: Difference between revisions
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==Binary complex of human polymerase nu and DNA with the finger domain closed and thumb domain rotated out== | ==Binary complex of human polymerase nu and DNA with the finger domain closed and thumb domain rotated out== | ||
<StructureSection load='4xvm' size='340' side='right' caption='[[4xvm]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='4xvm' size='340' side='right'caption='[[4xvm]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xvm]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xvm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XVM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</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=4xvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xvm OCA], [https://pdbe.org/4xvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xvm RCSB], [https://www.ebi.ac.uk/pdbsum/4xvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xvm ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DPOLN_HUMAN DPOLN_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4xvm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xvm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Lee | [[Category: Lee Y-S]] | ||
[[Category: Yang | [[Category: Yang W]] | ||
Latest revision as of 10:50, 27 September 2023
Binary complex of human polymerase nu and DNA with the finger domain closed and thumb domain rotated outBinary complex of human polymerase nu and DNA with the finger domain closed and thumb domain rotated out
Structural highlights
FunctionPublication Abstract from PubMedAll DNA replicases achieve high fidelity by a conserved mechanism, but each translesion polymerase carries out mutagenic DNA synthesis in its own way. Here we report crystal structures of human DNA polymerase nu (Pol nu), which is homologous to high-fidelity replicases yet is error prone. Instead of a simple open-to-closed movement of the O helix upon binding of a correct incoming nucleotide, Pol nu has a different open state and requires the finger domain to swing sideways and undergo both opening and closing motions to accommodate the nascent base pair. A single-amino acid substitution in the O helix of the finger domain improves the fidelity of Pol nu nearly ten-fold. A unique cavity and the flexibility of the thumb domain allow Pol nu to generate and accommodate a looped-out primer strand. Primer loop-out may be a mechanism for DNA trinucloetide-repeat expansion. How a homolog of high-fidelity replicases conducts mutagenic DNA synthesis.,Lee YS, Gao Y, Yang W Nat Struct Mol Biol. 2015 Mar 16. doi: 10.1038/nsmb.2985. PMID:25775266[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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