4f50: Difference between revisions

<StructureSection load='4f50' size='340' side='right' caption='[[4f50]], [[Resolution|resolution]] 2.21&Aring;' scene=''>

<table><tr><td colspan='2'>[[4f50]] is a 3 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=4F50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F50 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></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f4w|4f4w]], [[4f4x|4f4x]], [[4f4y|4f4y]], [[4f4z|4f4z]]</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=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='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=4f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f50 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f50 RCSB], [http://www.ebi.ac.uk/pdbsum/4f50 PDBsum]</span></td></tr>

== Publication Abstract from PubMed ==

Y-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<ref>PMID:23245850</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

*[[DNA polymerase|DNA polymerase]]

[[Category: DNA-directed DNA polymerase]]

[[Category: Sulso]]

[[Category: Pata, J D]]

[[Category: Wilson, R C]]

[[Category: Transferase-dna complex]]

[[Category: Y-family polymerase]]