5ktq
From Proteopedia
(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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| - | [[Image:5ktq.gif|left|200px]]<br /><applet load="5ktq" size=" | + | [[Image:5ktq.gif|left|200px]]<br /><applet load="5ktq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="5ktq, resolution 2.50Å" /> | caption="5ktq, resolution 2.50Å" /> | ||
'''LARGE FRAGMENT OF TAQ DNA POLYMERASE BOUND TO DCTP'''<br /> | '''LARGE FRAGMENT OF TAQ DNA POLYMERASE BOUND TO DCTP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of the Klenow fragment of the Thermus aquaticus DNA | + | 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== | ==About this Structure== | ||
| - | 5KTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with DCP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 5KTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=DCP:'>DCP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: large fragement of taq dna polymerase i]] | [[Category: large fragement of taq dna polymerase i]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:25 2008'' |
Revision as of 17:15, 21 February 2008
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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 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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