1GO8

The metzincin's methionine: PrtC M226L mutant

1GO8 の概要

• エントリーDOI: 10.2210/pdb1go8/pdb
• 関連するPDBエントリー: 1GO7
• 分子名称: PROTEASE C, CALCIUM ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, metalloprotease, protease
• 由来する生物種: ERWINIA CHRYSANTHEMI
• 細胞内の位置: Secreted: P16317
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50189.05

構造登録者

Baumann, U. (登録日: 2001-10-20, 公開日: 2002-10-17, 最終更新日: 2024-05-01)

主引用文献

Hege, T.,Feltzer, R.E.,Gray, R.D.,Baumann, U.
Crystal Structure of a Complex between Pseudomonas Aeruginosa Alkaline Protease and its Cognate Inhibitor: Inhibition by a Zinc-NH2 Coordinative Bond
J.Biol.Chem., 276:35087-, 2001

PubMed Abstract: Serralysins are a family of metalloproteases secreted by Gram-negative bacteria into the medium in the form of inactive zymogens. Usually, all serralysin secretors have on the same operon a gene coding for a periplasmic 10-kDa protein, which is an inhibitor of the secreted protease. The recent characterization of the inhibitor of the alkaline protease from Pseudomonas aeruginosa revealed a surprisingly low dissociation constant of 4 pm, contrary to earlier studies on homologous systems, where inhibition constants in the microm range were reported. To approach a more accurate understanding, the crystal structure of the complex between inhibitor and protease from P. aeruginosa was determined at 1.74 A resolution and refined to R(free) = 0.204. The structure reported here shows clearly that the N terminus of the inhibitor forms a coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc distance of 2.17 A. We conclude that this interaction adds substantially to the complex stability and show also that similar interactions are found in other metzincin-inhibitor complexes.

PubMed: 11445573
DOI: 10.1074/JBC.M104020200

実験手法

X-RAY DIFFRACTION (2 Å)