3WE2
Structure of BLM RQC domain bound to a phosphate ion
Summary for 3WE2
| Entry DOI | 10.2210/pdb3we2/pdb |
| Related | 3WE3 |
| Descriptor | Bloom syndrome protein, PHOSPHATE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | winged-helix, dna helicase, dna binding, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P54132 |
| Total number of polymer chains | 2 |
| Total formula weight | 32745.45 |
| Authors | Kim, S.Y.,Hakoshima, T.,Kitano, K. (deposition date: 2013-06-28, release date: 2013-11-13, Last modification date: 2024-03-20) |
| Primary citation | Kim, S.Y.,Hakoshima, T.,Kitano, K. Structure of the RecQ C-terminal Domain of Human Bloom Syndrome Protein Sci Rep, 3:3294-3294, 2013 Cited by PubMed Abstract: 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 β-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 β-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. PubMed: 24257077DOI: 10.1038/srep03294 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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