1HT3

MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THE ACTIVE SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTAL STRUCTURE OF THE COMPLEX OF A PARTIALLY MODIFIED PROTEINASE K WITH MERCURY AT 1.8 A RESOLUTION

1HT3 の概要

• エントリーDOI: 10.2210/pdb1ht3/pdb
• 関連するPDBエントリー: 1CNM 1EGQ 2PRK
• 分子名称: PROTEINASE K, MERCURY (II) ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: proteinase k, mercury, stereochemistry, hydrolase
• 由来する生物種: Engyodontium album
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29400.10

構造登録者

Gourinath, S. (登録日: 2000-12-27, 公開日: 2001-06-27, 最終更新日: 2024-10-30)

主引用文献

Gourinath, S.,Degenhardt, M.,Eschenburg, S.,Moore, K.,Delucas, L.J.,Betzel, C.H.,Singh, T.P.
Mercury induced modifications in the stereochemistry of the active site through Cys-73 in a serine protease--crystal structure of the complex of a partially modified proteinase K with mercury at 1.8 A resolution
Indian J.Biochem.Biophys., 38:298-302, 2001

PubMed Abstract: Proteinese K (PK) isolated from Tritirachium album Limber was crystallized with HgCl2 in excess, under microgravity conditions. The intensity data were collected at 4 degrees C to 1.8 A resolution and the final R-factor after refinement for all the reflections was 0.164. Mercury has been found at two sites with partial occupancies (0.4 and 0.6) which are at distances of 2.48 A and 2.58 A respectively from Cys-73 Sgamma. The Cys-73 in the enzyme structure is located close to the active site residue, His-69. This region is completely buried and is not accessible to the solvent. It is rather tightly packed. Therefore, the binding of mercury distorts the stereochemistry of the neighbouring residues including those belonging to the catalytic triad. As a result of this, the Ogamma of Ser-224 is displaced by 0.6 A which causes the inactivation of proteinase K by increasing the H-bond distance to 3.7 A between Ser-224 Ogamma and His-69 Nepsilon2.

PubMed: 11886076

実験手法

X-RAY DIFFRACTION (1.8 Å)