5ktq
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(New page: 200px<br /><applet load="5ktq" size="450" color="white" frame="true" align="right" spinBox="true" caption="5ktq, resolution 2.50Å" /> '''LARGE FRAGMENT OF TA...)
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Revision as of 17:27, 20 November 2007
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LARGE FRAGMENT OF TAQ DNA POLYMERASE BOUND TO DCTP
Overview
The crystal structures of the Klenow fragment of the Thermus aquaticus DNA, polymerase I (Klentaq1) complexed with four deoxyribonucleoside, triphosphates (dNTP) have been determined to 2.5 A resolution. The dNTPs, bind adjacent to the O helix of Klentaq1. The triphosphate moieties are at, nearly identical positions in all four complexes and are anchored by three, positively charged residues, Arg659, Lys663, and Arg587, and by two polar, residues, His639 and Gln613. The configuration of the base moieties in the, Klentaq1/dNTP complexes demonstrates variability suggesting that dNTP, binding is primarily determined by recognition and binding of the, phosphate moiety. However, when superimposed on the Taq polymerase/blunt, end DNA complex structure (Eom et al., 1996), two of the dNTP/Klentaq1, structures demonstrate appropriate stacking of the nucleotide base with, the 3' end of the DNA primer strand, suggesting that at least in these two, binary complexes, the observed dNTP conformations are functionally, relevant.
About this Structure
5KTQ is a Single protein structure of sequence from Thermus aquaticus with DCP as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates., Li Y, Kong Y, Korolev S, Waksman G, Protein Sci. 1998 May;7(5):1116-23. PMID:9605316
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