1kln
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(New page: 200px<br /> <applet load="1kln" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kln, resolution 3.200Å" /> '''DNA POLYMERASE I K...)
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Revision as of 06:55, 18 November 2007
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DNA POLYMERASE I KLENOW FRAGMENT (E.C.2.7.7.7) MUTANT/DNA COMPLEX
Overview
Klenow fragment of Escherichia coli DNA polymerase I, which was, cocrystallized with duplex DNA, positioned 11 base pairs of DNA in a, groove that lies at right angles to the cleft that contains the polymerase, active site and is adjacent to the 3' to 5' exonuclease domain. When the, fragment bound DNA, a region previously referred to as the "disordered, domain" became more ordered and moved along with two helices toward the 3', to 5' exonuclease domain to form the binding groove. A single-stranded, 3', extension of three nucleotides bound to the 3' to 5' exonuclease active, site. Although this cocrystal structure appears to be an editing complex, it suggests that the primer strand approaches the catalytic site of the, polymerase from the direction of the 3' to 5' exonuclease domain and that, the duplex DNA product may bend to enter the cleft that contains the, polymerase catalytic site.
About this Structure
1KLN is a Single protein structure of sequence from Escherichia coli with ZN as ligand. The following page contains interesting information on the relation of 1KLN with [DNA Polymerase]. Full crystallographic information is available from OCA.
Reference
Structure of DNA polymerase I Klenow fragment bound to duplex DNA., Beese LS, Derbyshire V, Steitz TA, Science. 1993 Apr 16;260(5106):352-5. PMID:8469987
Page seeded by OCA on Sun Nov 18 09:02:54 2007
