4EPD

Initial Urease Structure for Radiation Damage Experiment at 300 K

4EPD の概要

• エントリーDOI: 10.2210/pdb4epd/pdb
• 関連するPDBエントリー: 4EP8 4EPB 4EPE
• 分子名称: Urease subunit alpha, Urease subunit beta, Urease subunit gamma, ... (5 entities in total)
• 機能のキーワード: alpha-beta barrel, nickel metalloenzyme, hydrolase, radiation damage
• 由来する生物種: Enterobacter aerogenes; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P18314 P18315 P18316
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 82622.17

構造登録者

Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E. (登録日: 2012-04-17, 公開日: 2012-08-29, 最終更新日: 2013-01-23)

主引用文献

Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E.
Spatial distribution of radiation damage to crystalline proteins at 25-300 K.
Acta Crystallogr.,Sect.D, 68:1108-1117, 2012

PubMed Abstract: The spatial distribution of radiation damage (assayed by increases in atomic B factors) to thaumatin and urease crystals at temperatures ranging from 25 to 300 K is reported. The nature of the damage changes dramatically at approximately 180 K. Above this temperature the role of solvent diffusion is apparent in thaumatin crystals, as solvent-exposed turns and loops are especially sensitive. In urease, a flap covering the active site is the most sensitive part of the molecule and nearby loops show enhanced sensitivity. Below 180 K sensitivity is correlated with poor local packing, especially in thaumatin. At all temperatures, the component of the damage that is spatially uniform within the unit cell accounts for more than half of the total increase in the atomic B factors and correlates with changes in mosaicity. This component may arise from lattice-level, rather than local, disorder. The effects of primary structure on radiation sensitivity are small compared with those of tertiary structure, local packing, solvent accessibility and crystal contacts.

PubMed: 22948911
DOI: 10.1107/S0907444912021361

実験手法

X-RAY DIFFRACTION (1.7 Å)