4EL7

Initial Thaumatin Structure for Radiation Damage Experiment at 300 K

4EL7 の概要

• エントリーDOI: 10.2210/pdb4el7/pdb
• 関連するPDBエントリー: 4EK0 4EKA 4EKB 4EKH 4EKO 4EKT 4EL2 4EL3 4ELA
• 分子名称: Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: sweet protein, radiation damage, plant protein
• 由来する生物種: Thaumatococcus daniellii (katemfe)
• 細胞内の位置: Cytoplasmic vesicle: P02883
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22393.21

構造登録者

Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E. (登録日: 2012-04-10, 公開日: 2012-08-29, 最終更新日: 2024-10-09)

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 (1.52 Å)