3ktq
From Proteopedia
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CRYSTAL STRUCTURE OF AN ACTIVE TERNARY COMPLEX OF THE LARGE FRAGMENT OF DNA POLYMERASE I FROM THERMUS AQUATICUS
Overview
The crystal structures of two ternary complexes of the large fragment of, Thermus aquaticus DNA polymerase I (Klentaq1) with a primer/template DNA, and dideoxycytidine triphosphate, and that of a binary complex of the same, enzyme with a primer/template DNA, were determined to a resolution of 2.3, 2.3 and 2.5 A, respectively. One ternary complex structure differs, markedly from the two other structures by a large reorientation of the tip, of the fingers domain. This structure, designated 'closed', represents the, ternary polymerase complex caught in the act of incorporating a, nucleotide. In the two other structures, the tip of the fingers domain is, rotated outward by 46 degrees ('open') in an orientation similar to that, of the apo form of Klentaq1. These structures provide the first direct, evidence in DNA polymerase I enzymes of a large conformational change, responsible for assembling an active ternary complex.
About this Structure
3KTQ is a Single protein structure of sequence from Thermus aquaticus with MG and DCT as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation., Li Y, Korolev S, Waksman G, EMBO J. 1998 Dec 15;17(24):7514-25. PMID:9857206
Page seeded by OCA on Tue Nov 20 19:48:38 2007
