2XBR

Raman crystallography of Hen White Egg Lysozyme - Low X-ray dose (0.2 MGy)

2XBR の概要

• エントリーDOI: 10.2210/pdb2xbr/pdb
• 関連するPDBエントリー: 132L 193L 194L 1A2Y 1AKI 1AT5 1AT6 1AZF 1B0D 1B2K 1BGI 1BHZ 1BVK 1BVX 1BWH 1BWI 1BWJ 1C08 1C10 1DPW 1DPX 1DQJ 1E8L 1F0W 1F10 1F3J 1FDL 1FLQ 1FLU 1FLW 1FLY 1FN5 1G7H 1G7I 1G7J 1G7L 1G7M 1GPQ 1GWD 1GXV 1GXX 1H6M 1H87 1HC0 1HEL 1HEM 1HEN 1HEO 1HEP 1HEQ 1HER 1HEW 1HF4 1HSW 1HSX 1IC4 1IC5 1IC7 1IEE 1IO5 1IOQ 1IOR 1IOS 1IOT 1IR7 1IR8 1IR9 1J1O 1J1P 1J1X 1JA2 1JA4 1JA6 1JA7 1JIS 1JIT 1JIY 1JJ0 1JJ1 1JJ3 1JPO 1JTO 1JTT 1KIP 1KIQ 1KIR 1KXW 1KXX 1KXY 1LCN 1LJ3 1LJ4 1LJE 1LJF 1LJG 1LJH 1LJI 1LJJ 1LJK 1LKR 1LKS 1LMA 1LPI 1LSA 1LSB 1LSC 1LSD 1LSE 1LSF 1LSG 1LSM 1LSN 1LSY 1LSZ 1LYO 1LYS 1LYZ 1LZ8 1LZ9 1LZA 1LZB 1LZC 1LZD 1LZE 1LZG 1LZH 1LZN 1LZT 1MEL 1MLC 1N4F 1NBY 1NBZ 1NDG 1NDM 1P2C 1PS5 1QIO 1QTK 1RCM 1RFP 1RI8 1RJC 1SF4 1SF6 1SF7 1SFB 1SFG 1SQ2 1T3P 1T6V 1UA6 1UC0 1UCO 1UIA 1UIB 1UIC 1UID 1UIE 1UIF 1UIG 1UIH 1UUZ 1V7S 1V7T 1VAT 1VAU 1VDP 1VDQ 1VDS 1VDT 1VED 1VFB 1W6Z 1WTM 1WTN 1XEI 1XEJ 1XEK 1XFP 1XGP 1XGQ 1YIK 1YIL 1YKX 1YKY 1YKZ 1YL0 1YL1 1YQV 1Z55 1ZMY 2A6U 2A7D 2A7F 2AUB 2B5Z 2BLX 2BLY 2BPU 2C8O 2C8P 2CDS 2CGI 2D4I 2D4J 2D4K 2D6B 2D91 2FBB 2HFM 2IFF 2LYM 2LYO 2LYZ 2LZH 2LZT 2VB1 2W1L 2W1M 2W1X 2W1Y 2WAR 2X0A 2XBS 3HFM 3LYM 3LYO 3LYT 3LYZ 3LZT 4LYM 4LYO 4LYT 4LYZ 4LZT 5LYM 5LYT 5LYZ 6LYT 6LYZ 7LYZ 8LYZ
• 分子名称: LYSOZYME C, CHLORIDE ION (3 entities in total)
• 機能のキーワード: hydrolase, radiation damage, raman spectroscopy, disulfide radical
• 由来する生物種: GALLUS GALLUS (CHICKEN)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14614.78

構造登録者

Carpentier, P.,Royant, A.,Weik, M.,Bourgeois, D. (登録日: 2010-04-14, 公開日: 2010-11-24, 最終更新日: 2024-10-09)

主引用文献

Carpentier, P.,Royant, A.,Weik, M.,Bourgeois, D.
Raman Assisted Crystallography Reveals a Mechanism of X-Ray Induced Reversible Disulfide Radical Formation
Structure, 18:1410-, 2010

PubMed Abstract: X-ray-induced chemistry modifies biological macromolecules structurally and functionally, even at cryotemperatures. The mechanisms of x-radiation damage in colored or redox proteins have often been investigated by combining X-ray crystallography with in crystallo-ultraviolet-visible spectroscopy. Here, we used Raman microspectrophotometry to follow the onset of damage in crystalline lysozyme, notably that of disulfide bond breakage. The dose-dependent Raman spectra are consistent with a kinetic model for the rupture of disulfide bonds suggesting the rapid build up of an anionic radical intermediate. This intermediate may either revert back to the oxidized state or evolve toward protonated radical species or cleaved products. The data strongly suggest that back conversion of the anionic radical is significantly accelerated by X-rays, revealing an X-ray-induced "repair" mechanism. The possibility of X-ray-induced chemical repair is an important feature to take into account when assessing radiation damage in macromolecules.

PubMed: 21070940
DOI: 10.1016/J.STR.2010.09.010

実験手法

X-RAY DIFFRACTION (1.29 Å)