1dpi
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(New page: 200px<br /><applet load="1dpi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dpi, resolution 2.8Å" /> '''STRUCTURE OF LARGE FR...)
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Revision as of 11:21, 20 November 2007
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STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I COMPLEXED WITH D/TMP
Overview
The 3.3-A resolution crystal structure of the large proteolytic fragment, of Escherichia coli DNA polymerase I complexed with deoxythymidine, monophosphate consists of two domains, the smaller of which binds, zinc-deoxythymidine monophosphate. The most striking feature of the larger, domain is a deep crevice of the appropriate size and shape for binding, double-stranded B-DNA. A flexible subdomain may allow the enzyme to, surround completely the DNA substrate, thereby allowing processive, nucleotide polymerization without enzyme dissociation.
About this Structure
1DPI is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP., Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA, Nature. 1985 Feb 28-Mar 6;313(6005):762-6. PMID:3883192
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