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1ktq

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{{STRUCTURE_1ktq| PDB=1ktq | SCENE= }}
{{STRUCTURE_1ktq| PDB=1ktq | SCENE= }}
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'''DNA POLYMERASE'''
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===DNA POLYMERASE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_7568114}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_7568114}}
==About this Structure==
==About this Structure==
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[[Category: Dna-replication]]
[[Category: Dna-replication]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
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Revision as of 07:59, 2 July 2008

Image:1ktq.png

Template:STRUCTURE 1ktq

DNA POLYMERASE

Template:ABSTRACT PUBMED 7568114

About this Structure

1KTQ is a Single protein structure of sequence from Thermus aquaticus. 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

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