2BI3

Radiation damage of the Schiff base in phosphoserine aminotransferase (structure D)

2BI3 の概要

• エントリーDOI: 10.2210/pdb2bi3/pdb
• 関連するPDBエントリー: 1W23 2BHX 2BI1 2BI2 2BI5 2BI9 2BIA 2BIE 2BIG
• 分子名称: PHOSPHOSERINE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: transferase, aminotransferase, pyridoxal-5'-phosphate, radiation damage
• 由来する生物種: BACILLUS ALCALOPHILUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81777.07

構造登録者

Dubnovitsky, A.P.,Ravelli, R.B.G.,Popov, A.N.,Papageorgiou, A.C. (登録日: 2005-01-20, 公開日: 2005-05-19, 最終更新日: 2019-05-22)

主引用文献

Dubnovitsky, A.P.,Ravelli, R.B.G.,Popov, A.N.,Papageorgiou, A.C.
Strain Relief at the Active Site of Phosphoserine Aminotransferase Induced by Radiation Damage.
Protein Sci., 14:1498-, 2005

PubMed Abstract: The X-ray susceptibility of the lysine-pyridoxal-5'-phosphate Schiff base in Bacillus alcalophilus phosphoserine aminotransferase has been investigated using crystallographic data collected at 100 K to 1.3 A resolution, complemented by on-line spectroscopic studies. X-rays induce deprotonation of the internal aldimine, changes in the Schiff base conformation, displacement of the cofactor molecule, and disruption of the Schiff base linkage between pyridoxal-5'-phosphate and the Lys residue. Analysis of the "undamaged" structure reveals a significant chemical strain on the internal aldimine bond that leads to a pronounced geometrical distortion of the cofactor. However, upon crystal exposure to the X-rays, the strain and distortion are relaxed and eventually diminished when the total absorbed dose has exceeded 4.7 x 10(6) Ggamma. Our data provide new insights into the enzymatic activation of pyridoxal-5'-phosphate and suggest that special care should be taken while using macromolecular crystallography to study details in strained active sites.

PubMed: 15883191
DOI: 10.1110/PS.051397905

実験手法

X-RAY DIFFRACTION (1.69 Å)