Structure of HRDC domain from human Bloom syndrome protein, BLM
[BLM_HUMAN] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry.
[BLM_HUMAN] Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE).   
Publication Abstract from PubMed
Bloom syndrome is a rare genetic disorder characterized by severe growth retardation and cancer predisposition. The disease is caused by a loss of function of the Bloom syndrome protein (BLM), a member of the RecQ family of DNA helicases. Here we report on the first 3D structure of a BLM fragment, a solution structure of the C-terminal helicase-and-ribonuclease D-C-terminal (HRDC) domain from human BLM. The structure reveals unique features of BLM HRDC that are distinct from the HRDC domain of Werner syndrome protein. In particular, BLM HRDC retains many acidic residues exposed to the solvent, which makes the domain surface extensively electronegative. Consistent with this, fluorescence polarization assays showed an inability of isolated BLM HRDC to interact with DNA substrates. Analyses employing ultracentrifugation, gel-filtration, CD spectroscopy and dynamic light scattering showed that the BLM HRDC domain exists as a stable monomer in solution. The results show that BLM HRDC is a compact, robust and acidic motif which may play a distinct role apart from DNA binding.
Solution structure of the HRDC domain of human Bloom syndrome protein BLM.,Sato A, Mishima M, Nagai A, Kim SY, Ito Y, Hakoshima T, Jee JG, Kitano K J Biochem. 2010 Oct;148(4):517-25. Epub 2010 Aug 25. PMID:20739603
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.