4f4w: Difference between revisions
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==Y-family DNA polymerase chimera Dbh-Dpo4-Dpo4 #1== | ==Y-family DNA polymerase chimera Dbh-Dpo4-Dpo4 #1== | ||
<StructureSection load='4f4w' size='340' side='right' caption='[[4f4w]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4f4w' size='340' side='right' caption='[[4f4w]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f4w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4f4w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F4W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F4W FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f4x|4f4x]], [[4f4y|4f4y]], [[4f4z|4f4z]], [[4f50|4f50]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f4x|4f4x]], [[4f4y|4f4y]], [[4f4z|4f4z]], [[4f50|4f50]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dbh, dpo4, Dpo4 (S. solfataricus) and Dbh (S. acidocaldarius), Saci_0554, SSO2448 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dbh, dpo4, Dpo4 (S. solfataricus) and Dbh (S. acidocaldarius), Saci_0554, SSO2448 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</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=4f4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f4w RCSB], [http://www.ebi.ac.uk/pdbsum/4f4w PDBsum]</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=4f4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4w OCA], [http://pdbe.org/4f4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f4w RCSB], [http://www.ebi.ac.uk/pdbsum/4f4w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f4w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 4f4w" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: | [[Category: Sulso]] | ||
[[Category: Pata, J D]] | [[Category: Pata, J D]] | ||
[[Category: Wilson, R C]] | [[Category: Wilson, R C]] | ||
[[Category: Transferase-dna complex]] | [[Category: Transferase-dna complex]] | ||
[[Category: Y-family polymerase]] | [[Category: Y-family polymerase]] | ||
Revision as of 12:58, 5 August 2016
Y-family DNA polymerase chimera Dbh-Dpo4-Dpo4 #1Y-family DNA polymerase chimera Dbh-Dpo4-Dpo4 #1
Structural highlights
Function[DPO4_SULAC] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis (By similarity). Publication Abstract from PubMedY-family polymerases help cells tolerate DNA damage by performing translesion synthesis opposite damaged DNA bases, yet they also have a high intrinsic error rate. We constructed chimeras of two closely related Y-family polymerases that display distinctly different activity profiles and found that the polypeptide linker that tethers the catalytic polymerase domain to the C-terminal DNA-binding domain is a major determinant of overall polymerase activity, nucleotide incorporation fidelity, and abasic site-bypass ability. Exchanging just 3 out of the 15 linker residues is sufficient to interconvert the polymerase activities tested. Crystal structures of four chimeras show that the conformation of the protein correlates with the identity of the interdomain linker sequence. Thus, residues that are more than 15 A away from the active site are able to influence many aspects of polymerase activity by altering the relative orientations of the catalytic and DNA-binding domains. Y-Family Polymerase Conformation Is a Major Determinant of Fidelity and Translesion Specificity.,Wilson RC, Jackson MA, Pata JD Structure. 2012 Dec 11. pii: S0969-2126(12)00420-0. doi:, 10.1016/j.str.2012.11.005. PMID:23245850[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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