4xvi: Difference between revisions
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<StructureSection load='4xvi' size='340' side='right' caption='[[4xvi]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='4xvi' size='340' side='right' caption='[[4xvi]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xvi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XVI FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xvi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XVI FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xvk|4xvk]], [[4xvl|4xvl]], [[4xvm|4xvm]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xvk|4xvk]], [[4xvl|4xvl]], [[4xvm|4xvm]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">POLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></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=4xvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xvi OCA], [http://pdbe.org/4xvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xvi RCSB], [http://www.ebi.ac.uk/pdbsum/4xvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xvi ProSAT]</span></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=4xvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xvi OCA], [http://pdbe.org/4xvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xvi RCSB], [http://www.ebi.ac.uk/pdbsum/4xvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xvi ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4xvi" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xvi" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Human]] | |||
[[Category: Lee, Y S]] | [[Category: Lee, Y S]] | ||
[[Category: Yang, W]] | [[Category: Yang, W]] | ||
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[[Category: Pol nu]] | [[Category: Pol nu]] | ||
[[Category: Polymerase]] | [[Category: Polymerase]] | ||
[[Category: Transferase-dna complex]] | |||
Revision as of 15:17, 6 November 2017
Binary complex of human polymerase nu and DNA with the finger domain ajarBinary complex of human polymerase nu and DNA with the finger domain ajar
Structural highlights
Publication 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. References
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