Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate

Biochemistry ◽  
1993 ◽  
Vol 32 (51) ◽  
pp. 14095-14101 ◽  
Author(s):  
Lorena S. Beese ◽  
Jonathan M. Friedman ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structures ◽  
Dna Polymerase ◽  
Klenow Fragment ◽  
Dna Polymerase I ◽  
Deoxynucleoside Triphosphate ◽  
Polymerase I

Uracil Glycol Deoxynucleoside Triphosphate Is a Better Substrate for DNA Polymerase I Klenow Fragment Than Thymine Glycol Deoxynucleoside Triphosphate†

Biochemistry ◽  
1998 ◽  
Vol 37 (1) ◽  
pp. 330-338 ◽  
Author(s):  
Andrei A. Purmal ◽  
Jeffrey P. Bond ◽  
Barbara A. Lyons ◽  
Yoke Wah Kow ◽  
Susan S. Wallace
Keyword(s):  
Dna Polymerase ◽  
Klenow Fragment ◽  
Dna Polymerase I ◽  
Thymine Glycol ◽  
Deoxynucleoside Triphosphate ◽  
Polymerase I

scholarly journals Processive Incorporation of Deoxynucleoside Triphosphate Analogs by Single-Molecule DNA Polymerase I (Klenow Fragment) Nanocircuits

2015 ◽  
Vol 137 (30) ◽  
pp. 9587-9594 ◽  
Author(s):  
Kaitlin M. Pugliese ◽  
O. Tolga Gul ◽  
Yongki Choi ◽  
Tivoli J. Olsen ◽  
Patrick C. Sims ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Single Molecule ◽  
Klenow Fragment ◽  
Dna Polymerase I ◽  
Deoxynucleoside Triphosphate ◽  
Polymerase I

scholarly journals Crystallization and preliminary X-ray analysis of thePlasmodium falciparumapicoplast DNA polymerase

2015 ◽  
Vol 71 (3) ◽  
pp. 333-337 ◽  
Author(s):  
Morgan E. Milton ◽  
Jun-yong Choe ◽  
Richard B. Honzatko ◽  
Scott W. Nelson
Keyword(s):  
Dna Polymerase ◽  
Structural Information ◽  
Klenow Fragment ◽  
X Ray Diffraction ◽  
Dna Polymerase I ◽  
X Ray ◽  
Cell Parameters ◽  
A Genome ◽  
Reported Data ◽  
Polymerase I

Infection by the parasitePlasmodium falciparumis the leading cause of malaria in humans. The parasite has a unique and essential plastid-like organelle called the apicoplast. The apicoplast contains a genome that undergoes replication and repair through the action of a replicative polymerase (apPOL). apPOL has no direct orthologs in mammalian polymerases and is therefore an attractive antimalarial drug target. No structural information exists for apPOL, and the Klenow fragment ofEscherichia coliDNA polymerase I, which is its closest structural homolog, shares only 28% sequence identity. Here, conditions for the crystallization of and preliminary X-ray diffraction data from crystals ofP. falciparumapPOL are reported. Data complete to 3.5 Å resolution were collected from a single crystal (2 × 2 × 5 µm) using a 5 µm beam. The space groupP6522 (unit-cell parametersa=b= 141.8,c= 149.7 Å, α = β = 90, γ = 120°) was confirmed by molecular replacement. Refinement is in progress.

scholarly journals Crystal structures of DNA polymerase I capture novel intermediates in the DNA synthesis pathway

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Nicholas Chim ◽  
Lynnette N Jackson ◽  
Anh M Trinh ◽  
John C Chaput
Keyword(s):  
High Resolution ◽  
Dna Synthesis ◽  
Crystal Structures ◽  
Dna Polymerase ◽  
Active Site ◽  
Dna Polymerase I ◽  
Dynamic Nature ◽  
Enzyme Active Site ◽  
Polymerase I ◽  
In Cells

High resolution crystal structures of DNA polymerase intermediates are needed to study the mechanism of DNA synthesis in cells. Here we report five crystal structures of DNA polymerase I that capture new conformations for the polymerase translocation and nucleotide pre-insertion steps in the DNA synthesis pathway. We suggest that these new structures, along with previously solved structures, highlight the dynamic nature of the finger subdomain in the enzyme active site.

How E. coli DNA polymerase I (klenow fragment) distinguishes between deoxy- and dideoxynucleotides

1998 ◽  
Vol 278 (1) ◽  
pp. 147-165 ◽  
Author(s):  
Mekbib Astatke ◽  
Nigel D.F Grindley ◽  
Catherine M Joyce
Keyword(s):  
Dna Polymerase ◽  
Klenow Fragment ◽  
Dna Polymerase I ◽  
E Coli ◽  
Polymerase I
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