 |
PDBsum entry 3ktq
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transferase/DNA
|
PDB id
|
|
|
|
3ktq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
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.
|
 |
|
Authors
|
 |
Y.Li,
S.Korolev,
G.Waksman.
|
 |
|
Ref.
|
 |
Embo J, 1998,
17,
7514-7525.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
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.
|
 |
|
|
|
|
 |