3we3

Structure of BLM RQC domain bound to an arsenate ion

spinqualitylabelsall models 3we3, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3we3 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, ART Related: 3we2 Gene: BLM (HUMAN) Activity: DNA helicase, with EC number 3.6.4.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [BLM_HUMAN] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry. Function [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 genomic instability and cancer predisposition. The disease is caused by mutations of the Bloom syndrome protein (BLM). Here we report the crystal structure of a RecQ C-terminal (RQC) domain from human BLM. The structure reveals three novel features of BLM RQC which distinguish it from the previous structures of the Werner syndrome protein (WRN) and RECQ1. First, BLM RQC lacks an aromatic residue at the tip of the beta-wing, a key element of the RecQ-family helicases used for DNA-strand separation. Second, a BLM-specific insertion between the N-terminal helices exhibits a looping-out structure that extends at right angles to the beta-wing. Deletion mutagenesis of this insertion interfered with binding to Holliday junction. Third, the C-terminal region of BLM RQC adopts an extended structure running along the domain surface, which may facilitate the spatial positioning of an HRDC domain in the full-length protein. Structure of the RecQ C-terminal Domain of Human Bloom Syndrome Protein.,Kim SY, Hakoshima T, Kitano K Sci Rep. 2013 Nov 21;3:3294. doi: 10.1038/srep03294. PMID:24257077 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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