2MH9: Resonance assignment of RQC domain of human Bloom syndrome protein

Citation:
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 (alpha1-alpha2 loop and alpha3 region), and the aromatic side chain on the top of the beta-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.
PDB ID: 2MH9Download
MMDB ID: 124262
PDB Deposition Date: 2013/11/19
Updated in MMDB: 2014/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MH9: monomeric; determined by author
Molecular Components in 2MH9
Label Count Molecule
Protein (1 molecule)
1
Bloom Syndrome Protein(Gene symbol: BLM)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.