3UV0: Crystal Structure Of The Drosophila Mu2 Fha Domain

Mutator 2 (MU2) in Drosophila melanogaster has been proposed to be the ortholog of human MDC1, a key mediator in DNA damage response. The forkhead-associated (FHA) domain of MDC1 is a dimerization module regulated by trans binding to phosphothreonine 4 from another molecule. Here we present the crystal structure of the MU2 FHA domain at 1.9A resolution, revealing its evolutionarily conserved role in dimerization. As compared to the MDC1 FHA domain, the MU2 FHA domain dimerizes using a different and more stable interface and contains a degenerate phosphothreonine-binding pocket. Our results suggest that the MU2 dimerization is constitutive and lacks phosphorylation-mediated regulation.
PDB ID: 3UV0Download
MMDB ID: 96769
PDB Deposition Date: 2011/11/29
Updated in MMDB: 2014/03
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3UV0: dimeric; determined by author and by software (PISA)
Molecular Components in 3UV0
Label Count Molecule
Proteins (2 molecules)
Mutator 2, Isoform B
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB