1QIO

SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE CAUSED BY INTENSE SYNCHROTRON RADIATION TO HEN EGG WHITE LYSOZYME

1QIO の概要

• エントリーDOI: 10.2210/pdb1qio/pdb
• 分子名称: LYSOZYME, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: radiation damages, disulfide bond, hydrolase (o-glycosyl), hydrolase
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14425.06

構造登録者

Kryger, G.,Weik, M.,Ravelli, R.B. (登録日: 1999-06-14, 公開日: 2001-04-11, 最終更新日: 2024-10-30)

主引用文献

Weik, M.,Ravelli, R.B.,Kryger, G.,McSweeney, S.,Raves, M.L.,Harel, M.,Gros, P.,Silman, I.,Kroon, J.,Sussman, J.L.
Specific chemical and structural damage to proteins produced by synchrotron radiation.
Proc.Natl.Acad.Sci.USA, 97:623-628, 2000

PubMed Abstract: Radiation damage is an inherent problem in x-ray crystallography. It usually is presumed to be nonspecific and manifested as a gradual decay in the overall quality of data obtained for a given crystal as data collection proceeds. Based on third-generation synchrotron x-ray data, collected at cryogenic temperatures, we show for the enzymes Torpedo californica acetylcholinesterase and hen egg white lysozyme that synchrotron radiation also can cause highly specific damage. Disulfide bridges break, and carboxyl groups of acidic residues lose their definition. Highly exposed carboxyls, and those in the active site of both enzymes, appear particularly susceptible. The catalytic triad residue, His-440, in acetylcholinesterase, also appears to be much more sensitive to radiation damage than other histidine residues. Our findings have direct practical implications for routine x-ray data collection at high-energy synchrotron sources. Furthermore, they provide a direct approach for studying the radiation chemistry of proteins and nucleic acids at a detailed, structural level and also may yield information concerning putative "weak links" in a given biological macromolecule, which may be of structural and functional significance.

PubMed: 10639129
DOI: 10.1073/pnas.97.2.623

実験手法

X-RAY DIFFRACTION (1.2 Å)