Cyclobutane thymine dimer (blue) and the flipped-out adenine base (red) C O N S Highlights the 60 degree kink formed by the DNA (space-filled) as it sits in the catalytic site of the enzyme(wireframe) On average, the helical twist is 35.4 degrees. Two base pairs, G-C & G-C, on the 3'-side of the flipped out adenine, exhibit a helical twist of 26.9 degrees. Formation of a large "hole" (10A x 9A x 7A) between bases above and below the flipped out adenine Near the carboxy terminus, a conformational change appears to be connected to the movements of the Arg-125 and Trp-128 side chains(red), which are induced by binding to DNA. This loop partly overlaps the WYKYY (128-132) segment, which participates in DNA binding Residues 83-91(red)--These residues are disordered when the enzyme is free of a substrate, but become well-defined when bound to DNA (green) Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
Highlights the 60 degree kink formed by the DNA (space-filled) as it sits in the catalytic site of the enzyme(wireframe) On average, the helical twist is 35.4 degrees. Two base pairs, G-C & G-C, on the 3'-side of the flipped out adenine, exhibit a helical twist of 26.9 degrees. Formation of a large "hole" (10A x 9A x 7A) between bases above and below the flipped out adenine Near the carboxy terminus, a conformational change appears to be connected to the movements of the Arg-125 and Trp-128 side chains(red), which are induced by binding to DNA. This loop partly overlaps the WYKYY (128-132) segment, which participates in DNA binding Residues 83-91(red)--These residues are disordered when the enzyme is free of a substrate, but become well-defined when bound to DNA (green) Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
On average, the helical twist is 35.4 degrees. Two base pairs, G-C & G-C, on the 3'-side of the flipped out adenine, exhibit a helical twist of 26.9 degrees. Formation of a large "hole" (10A x 9A x 7A) between bases above and below the flipped out adenine Near the carboxy terminus, a conformational change appears to be connected to the movements of the Arg-125 and Trp-128 side chains(red), which are induced by binding to DNA. This loop partly overlaps the WYKYY (128-132) segment, which participates in DNA binding Residues 83-91(red)--These residues are disordered when the enzyme is free of a substrate, but become well-defined when bound to DNA (green) Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
Formation of a large "hole" (10A x 9A x 7A) between bases above and below the flipped out adenine Near the carboxy terminus, a conformational change appears to be connected to the movements of the Arg-125 and Trp-128 side chains(red), which are induced by binding to DNA. This loop partly overlaps the WYKYY (128-132) segment, which participates in DNA binding Residues 83-91(red)--These residues are disordered when the enzyme is free of a substrate, but become well-defined when bound to DNA (green) Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
Near the carboxy terminus, a conformational change appears to be connected to the movements of the Arg-125 and Trp-128 side chains(red), which are induced by binding to DNA. This loop partly overlaps the WYKYY (128-132) segment, which participates in DNA binding Residues 83-91(red)--These residues are disordered when the enzyme is free of a substrate, but become well-defined when bound to DNA (green) Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
Residues 83-91(red)--These residues are disordered when the enzyme is free of a substrate, but become well-defined when bound to DNA (green) Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
Polar Interactions between T4 Endo V (3'-side of PD in red and 5'-side in blue) and DNA backbone Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
Van der Waals contacts around flipped-out adenine base UtilitiesColor Schemes Next: T4 endonuclease V (Part II) How to install your own scripts into this template.
UtilitiesColor Schemes
Next: T4 endonuclease V (Part II)
How to install your own scripts into this template.