4X4C

RADIATION DAMAGE TO THE NUCLEOPROTEIN COMPLEX C.Esp1396I: DOSE (DWD) 6.2 MGy

4X4C の概要

• エントリーDOI: 10.2210/pdb4x4c/pdb
• 関連するPDBエントリー: 3CLC 4X4B
• 分子名称: Regulatory protein, 35-MER DNA (3 entities in total)
• 機能のキーワード: protein-dna complex, radiation damage, gene regulation
• 由来する生物種: Enterobacter sp. RFL1396; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 59615.63

構造登録者

Bury, C.S.,McGeehan, J.E.,Garman, E.F. (登録日: 2014-12-02, 公開日: 2015-03-11, 最終更新日: 2024-01-10)

主引用文献

Bury, C.,Garman, E.F.,Ginn, H.M.,Ravelli, R.B.,Carmichael, I.,Kneale, G.,McGeehan, J.E.
Radiation damage to nucleoprotein complexes in macromolecular crystallography.
J.Synchrotron Radiat., 22:213-224, 2015

PubMed Abstract: Significant progress has been made in macromolecular crystallography over recent years in both the understanding and mitigation of X-ray induced radiation damage when collecting diffraction data from crystalline proteins. In contrast, despite the large field that is productively engaged in the study of radiation chemistry of nucleic acids, particularly of DNA, there are currently very few X-ray crystallographic studies on radiation damage mechanisms in nucleic acids. Quantitative comparison of damage to protein and DNA crystals separately is challenging, but many of the issues are circumvented by studying pre-formed biological nucleoprotein complexes where direct comparison of each component can be made under the same controlled conditions. Here a model protein-DNA complex C.Esp1396I is employed to investigate specific damage mechanisms for protein and DNA in a biologically relevant complex over a large dose range (2.07-44.63 MGy). In order to allow a quantitative analysis of radiation damage sites from a complex series of macromolecular diffraction data, a computational method has been developed that is generally applicable to the field. Typical specific damage was observed for both the protein on particular amino acids and for the DNA on, for example, the cleavage of base-sugar N1-C and sugar-phosphate C-O bonds. Strikingly the DNA component was determined to be far more resistant to specific damage than the protein for the investigated dose range. At low doses the protein was observed to be susceptible to radiation damage while the DNA was far more resistant, damage only being observed at significantly higher doses.

PubMed: 25723923
DOI: 10.1107/S1600577514026289

実験手法

X-RAY DIFFRACTION (2.8 Å)