Mre11 Rad50 binding domain in complex with Rad50 and AMP-PNP

PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER

ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair.

Kohzu Dual Double Crystal Monochromator (DDCM) Si(111)

DNA double-strand break repair rad50 ATPase

DNA double-strand break repair protein mre11
Rad50 binding domain (UNP residues 348-381)

MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGT
KYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVREV
LNLDKFETAYKKLSELKKTINNRIKEYGGSGGIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGK
YSEVVVRAEENKVRLFVVWEGKERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERY
LKKIPQVILVSHDEELKDAADHVIRISLENGSSKVEVVS

100 mM Tris, 200-300 mM lithium sulfate, 12-13% PEG3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

THE RAD50 ABC-ATPASE CONSTRUCT CONSISTS OF UNP RESIDUES 1-187 AND 716-882 CONNECTED BY AN ENGINEERED LINKER (GGSGG)

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

RecA-like fold, coiled-coils, ATPase, exonuclease, endonuclease, ATP binding, DNA binding, REPLICATION

MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGT
KYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVREV
LNLDKFETAYKKLSELKKTINNRIKEY

IKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENKVRLFVVWEGKERPLTFLSGG
ERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRISLENGS
SKVEVVS