2MH9
Resonance assignment of RQC domain of human Bloom syndrome protein
Summary for 2MH9
| Entry DOI | 10.2210/pdb2mh9/pdb |
| NMR Information | BMRB: 19530 |
| Descriptor | Bloom syndrome protein (1 entity in total) |
| Functional Keywords | winged helix, rqc, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus : P54132 |
| Total number of polymer chains | 1 |
| Total formula weight | 16115.53 |
| Authors | Ko, J.,Ryu, K.S.,Choi, B.S. (deposition date: 2013-11-19, release date: 2014-10-29, Last modification date: 2024-05-15) |
| Primary citation | Park, C.J.,Ko, J.,Ryu, K.S.,Choi, B.S. Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein. J.Biomol.Nmr, 58:141-147, 2014 Cited by PubMed Abstract: RecQ C-terminal (RQC) domain is known as the main DNA binding module of RecQ helicases such as Bloom syndrome protein (BLM) and Werner syndrome protein (WRN) that recognizes various DNA structures. Even though BLM is able to resolve various DNA structures similarly to WRN, BLM has different binding preferences for DNA substrates from WRN. In this study, we determined the solution structure of the RQC domain of human BLM. The structure shares the common winged-helix motif with other RQC domains. However, half of the N-terminal has unstructured regions (α1-α2 loop and α3 region), and the aromatic side chain on the top of the β-hairpin, which is important for DNA duplex strand separation in other RQC domains, is substituted with a negatively charged residue (D1165) followed by the polar residue (Q1166). The structurally distinctive features of the RQC domain of human BLM suggest that the DNA binding modes of the BLM RQC domain may be different from those of other RQC domains. PubMed: 24435566DOI: 10.1007/s10858-014-9812-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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