Crystal Structure of DNA Recombination Protein RuvA and a Model for Its Binding to the Holliday Junction

Science ◽  
1996 ◽  
Vol 274 (5286) ◽  
pp. 415-421 ◽  
Author(s):  
J. B. Rafferty ◽  
S. E. Sedelnikova ◽  
D. Hargreaves ◽  
P. J. Artymiuk ◽  
P. J. Baker ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Recombination ◽  
Holliday Junction ◽  
Recombination Protein

scholarly journals The Order of Strand Exchanges in Cre-LoxP Recombination and its Basis Suggested by the Crystal Structure of a Cre-LoxP Holliday Junction Complex

2002 ◽  
Vol 319 (1) ◽  
pp. 107-127 ◽  
Author(s):  
Shelley S. Martin ◽  
Erik Pulido ◽  
Victor C. Chu ◽  
Tyson S. Lechner ◽  
Enoch P. Baldwin
Keyword(s):  
Crystal Structure ◽  
Holliday Junction

scholarly journals Crystal structure of RuvC resolvase in complex with Holliday junction substrate

2013 ◽  
Vol 41 (21) ◽  
pp. 9945-9955 ◽  
Author(s):  
Karolina M. Górecka ◽  
Weronika Komorowska ◽  
Marcin Nowotny
Keyword(s):  
Crystal Structure ◽  
Holliday Junction

scholarly journals Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8

2001 ◽  
Vol 98 (4) ◽  
pp. 1442-1447 ◽  
Author(s):  
K. Yamada ◽  
N. Kunishima ◽  
K. Mayanagi ◽  
T. Ohnishi ◽  
T. Nishino ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermus Thermophilus ◽  
Motor Protein ◽  
Holliday Junction ◽  
Thermus Thermophilus Hb8

scholarly journals Step-arrest mutants of FLP recombinase: implications for the catalytic mechanism of DNA recombination.

1988 ◽  
Vol 8 (8) ◽  
pp. 3303-3310 ◽  
Author(s):  
R L Parsons ◽  
P V Prasad ◽  
R M Harshey ◽  
M Jayaram
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Recognition ◽  
Dna Recombination ◽  
Indirect Evidence ◽  
Holliday Junction ◽  
Genetic Dissection ◽  
Yeast Plasmid ◽  
Site Specific ◽  
Flp Recombinase ◽  
The Family

The site-specific recombinase (FLP) encoded by the yeast plasmid 2 micron circle belongs to the integrase (of phage lambda) family of recombinases. The sparse homology within the members of this family contrasts with the invariance of three residues, His-396, Arg-399, and Tyr-433 (the numbers correspond to the family alignment positions), among them. We report here results on substrate recognition and catalysis by FLP proteins altered at these residues. Mutations of the conserved His and Tyr that aborted the reaction at specific steps of catalysis permitted genetic dissection of the possible biochemical steps of recombination. We provide indirect evidence that recombination by FLP proceeds through a Holliday junction intermediate.

CRYSTAL STRUCTURE OF BACTERIOPHAGE T7 ENDONUCLEASE I: A HOLLIDAY JUNCTION RESOLVING ENZYME

2000 ◽  
Vol 28 (3) ◽  
pp. A96-A96
Author(s):  
J.M. Hadden ◽  
M.A. Convery ◽  
A.-C. Declais ◽  
D.M.J. Lilley ◽  
S.E.V. Phillips
Keyword(s):  
Crystal Structure ◽  
Holliday Junction ◽  
Bacteriophage T7
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