1ktq
From Proteopedia
(New page: 200px<br /><applet load="1ktq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ktq, resolution 2.5Å" /> '''DNA POLYMERASE'''<br ...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1ktq.jpg|left|200px]]<br /><applet load="1ktq" size=" | + | [[Image:1ktq.jpg|left|200px]]<br /><applet load="1ktq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ktq, resolution 2.5Å" /> | caption="1ktq, resolution 2.5Å" /> | ||
'''DNA POLYMERASE'''<br /> | '''DNA POLYMERASE'''<br /> | ||
==Overview== | ==Overview== | ||
- | The crystal structure of the large fragment of the Thermus aquaticus DNA | + | The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain is identical in fold to the equivalent region of the Klenow fragment of Escherichia coli DNA polymerase I (Klenow pol I). Although the N-terminal domain of Klentaq1 differs greatly in sequence from its counterpart in Klenow pol I, it has clearly evolved from a common ancestor. The structure of Klentaq1 reveals the strategy utilized by this protein to maintain activity at high temperatures and provides the structural basis for future improvements of the enzyme. |
==About this Structure== | ==About this Structure== | ||
- | 1KTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. 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:// | + | 1KTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. 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=1KTQ OCA]. |
==Reference== | ==Reference== | ||
Line 19: | Line 19: | ||
[[Category: nucleotidyltransferase]] | [[Category: nucleotidyltransferase]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:52 2008'' |
Revision as of 11:37, 21 February 2008
|
DNA POLYMERASE
Overview
The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain is identical in fold to the equivalent region of the Klenow fragment of Escherichia coli DNA polymerase I (Klenow pol I). Although the N-terminal domain of Klentaq1 differs greatly in sequence from its counterpart in Klenow pol I, it has clearly evolved from a common ancestor. The structure of Klentaq1 reveals the strategy utilized by this protein to maintain activity at high temperatures and provides the structural basis for future improvements of the enzyme.
About this Structure
1KTQ is a Single protein structure of sequence from Thermus aquaticus. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability., Korolev S, Nayal M, Barnes WM, Di Cera E, Waksman G, Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9264-8. PMID:7568114
Page seeded by OCA on Thu Feb 21 13:37:52 2008