4D2I

Crystal structure of the HerA hexameric DNA translocase from Sulfolobus solfataricus bound to AMP-PNP

4D2I の概要

• エントリーDOI: 10.2210/pdb4d2i/pdb
• 分子名称: HERA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, nura, helicase, translocase, dna, mre11, rad50, homologous recombination
• 由来する生物種: SULFOLOBUS SOLFATARICUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112861.00

構造登録者

Rzechorzek, N.J.,Blackwood, J.K.,Bray, S.M.,Maman, J.D.,Pellegrini, L.,Robinson, N.P. (登録日: 2014-05-09, 公開日: 2014-12-03, 最終更新日: 2024-05-08)

主引用文献

Rzechorzek, N.J.,Blackwood, J.K.,Bray, S.M.,Maman, J.D.,Pellegrini, L.,Robinson, N.P.
Structure of the Hexameric Hera ATPase Reveals a Mechanism of Translocation-Coupled DNA-End Processing in Archaea
Nat.Commun., 5:5506-, 2014

PubMed Abstract: The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine.

PubMed: 25420454
DOI: 10.1038/NCOMMS6506

実験手法

X-RAY DIFFRACTION (2.841 Å)