4CDG

Crystal structure of the Bloom's syndrome helicase BLM in complex with Nanobody

4CDG の概要

• エントリーDOI: 10.2210/pdb4cdg/pdb
• 分子名称: BLOOM SYNDROME PROTEIN, NANOBODY, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus : P54132
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 186736.26

構造登録者

Newman, J.A.,Savitsky, P.,Allerston, C.K.,Pike, A.C.W.,Pardon, E.,Steyaert, J.,Arrowsmith, C.H.,von Delft, F.,Bountra, C.,Edwards, A.,Gileadi, O. (登録日: 2013-10-31, 公開日: 2013-11-13, 最終更新日: 2024-11-13)

主引用文献

Newman, J.A.,Savitsky, P.,Allerston, C.K.,Bizard, A.H.,Ozer, O.,Sarlos, K.,Liu, Y.,Pardon, E.,Steyaert, J.,Hickson, I.D.,Gileadi, O.
Crystal Structure of the Bloom'S Syndrome Helicase Indicates a Role for the Hrdc Domain in Conformational Changes.
Nucleic Acids Res., 43:5221-, 2015

PubMed Abstract: Bloom's syndrome helicase (BLM) is a member of the RecQ family of DNA helicases, which play key roles in the maintenance of genome integrity in all organism groups. We describe crystal structures of the BLM helicase domain in complex with DNA and with an antibody fragment, as well as SAXS and domain association studies in solution. We show an unexpected nucleotide-dependent interaction of the core helicase domain with the conserved, poorly characterized HRDC domain. The BLM-DNA complex shows an unusual base-flipping mechanism with unique positioning of the DNA duplex relative to the helicase core domains. Comparison with other crystal structures of RecQ helicases permits the definition of structural transitions underlying ATP-driven helicase action, and the identification of a nucleotide-regulated tunnel that may play a role in interactions with complex DNA substrates.

PubMed: 25901030
DOI: 10.1093/NAR/GKV373

実験手法

X-RAY DIFFRACTION (2.794 Å)