1nk5
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1nk5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nk5, resolution 2.10Å" /> '''ADENINE-ADENINE MISM...)
Next diff →
Revision as of 21:09, 24 November 2007
|
ADENINE-ADENINE MISMATCH AT THE POLYMERASE ACTIVE SITE
Overview
Accurate DNA replication is essential for genomic stability. One mechanism, by which high-fidelity DNA polymerases maintain replication accuracy, involves stalling of the polymerase in response to covalent incorporation, of mismatched base pairs, thereby favoring subsequent mismatch excision., Some polymerases retain a "short-term memory" of replication errors, responding to mismatches up to four base pairs in from the primer, terminus. Here we a present a structural characterization of all 12, possible mismatches captured at the growing primer terminus in the active, site of a polymerase. Our observations suggest four mechanisms that lead, to mismatch-induced stalling of the polymerase. Furthermore, we have, observed the effects of extending a mismatch up to six base pairs from the, primer terminus and find that long-range distortions in the DNA transmit, the presence of the mismatch back to the enzyme active site, suggesting, the structural basis for the short-term memory of replication errors.
About this Structure
1NK5 is a Protein complex structure of sequences from Geobacillus stearothermophilus with SUC, MG and SO4 as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Structures of mismatch replication errors observed in a DNA polymerase., Johnson SJ, Beese LS, Cell. 2004 Mar 19;116(6):803-16. PMID:15035983
Page seeded by OCA on Sat Nov 24 23:17:09 2007
