5JRJ

Crystal Structure of Herbaspirillum seropedicae RecA

5JRJ の概要

• エントリーDOI: 10.2210/pdb5jrj/pdb
• 分子名称: Protein RecA, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: dna-binding protein, atp-dependent dna protein, atpase activity, dna strand exchange, dna binding protein
• 由来する生物種: Herbaspirillum seropedicae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38490.98

構造登録者

Leite, W.C.,Galvao, C.W.,Saab, S.C.,Iulek, J.,Etto, R.M.,Steffens, M.B.R.,Chitteni-Pattu, S.,Stanage, T.,Keck, J.L.,Cox, M.M. (登録日: 2016-05-06, 公開日: 2016-08-03, 最終更新日: 2023-09-27)

主引用文献

Leite, W.C.,Galvao, C.W.,Saab, S.C.,Iulek, J.,Etto, R.M.,Steffens, M.B.,Chitteni-Pattu, S.,Stanage, T.,Keck, J.L.,Cox, M.M.
Structural and Functional Studies of H. seropedicae RecA Protein - Insights into the Polymerization of RecA Protein as Nucleoprotein Filament.
PLoS ONE, 11:e0159871-e0159871, 2016

PubMed Abstract: The bacterial RecA protein plays a role in the complex system of DNA damage repair. Here, we report the functional and structural characterization of the Herbaspirillum seropedicae RecA protein (HsRecA). HsRecA protein is more efficient at displacing SSB protein from ssDNA than Escherichia coli RecA protein. HsRecA also promotes DNA strand exchange more efficiently. The three dimensional structure of HsRecA-ADP/ATP complex has been solved to 1.7 Å resolution. HsRecA protein contains a small N-terminal domain, a central core ATPase domain and a large C-terminal domain, that are similar to homologous bacterial RecA proteins. Comparative structural analysis showed that the N-terminal polymerization motif of archaeal and eukaryotic RecA family proteins are also present in bacterial RecAs. Reconstruction of electrostatic potential from the hexameric structure of HsRecA-ADP/ATP revealed a high positive charge along the inner side, where ssDNA is bound inside the filament. The properties of this surface may explain the greater capacity of HsRecA protein to bind ssDNA, forming a contiguous nucleoprotein filament, displace SSB and promote DNA exchange relative to EcRecA. Our functional and structural analyses provide insight into the molecular mechanisms of polymerization of bacterial RecA as a helical nucleoprotein filament.

PubMed: 27447485
DOI: 10.1371/journal.pone.0159871

実験手法

X-RAY DIFFRACTION (1.7 Å)