2MH9

Resonance assignment of RQC domain of human Bloom syndrome protein

2MH9 の概要

• エントリーDOI: 10.2210/pdb2mh9/pdb
• NMR情報: BMRB: 19530
• 分子名称: Bloom syndrome protein (1 entity in total)
• 機能のキーワード: winged helix, rqc, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : P54132
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16115.53

構造登録者

Ko, J.,Ryu, K.S.,Choi, B.S. (登録日: 2013-11-19, 公開日: 2014-10-29, 最終更新日: 2024-05-15)

主引用文献

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

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: 24435566
DOI: 10.1007/s10858-014-9812-8

実験手法

SOLUTION NMR