1BZX

THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR

1BZX の概要

• エントリーDOI: 10.2210/pdb1bzx/pdb
• 分子名称: PROTEIN (TRYPSIN), PROTEIN (BOVINE PANCREATIC TRYPSIN INHIBITOR), CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: trypsin, serine proteinases, cold adaptation, inhibitor, substrate specificity, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Salmo salar (Atlantic salmon); 詳細
• 細胞内の位置: Secreted, extracellular space: P35031; Secreted: P00974
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30429.41

構造登録者

Helland, R.,Leiros, I.,Berglund, G.I.,Willassen, N.P.,Smalas, A.O. (登録日: 1998-11-05, 公開日: 1998-11-11, 最終更新日: 2024-11-20)

主引用文献

Helland, R.,Leiros, I.,Berglund, G.I.,Willassen, N.P.,Smalas, A.O.
The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor.
Eur.J.Biochem., 256:317-324, 1998

PubMed Abstract: The complex formed between anionic salmon trypsin (ST) and bovine pancreatic trypsin inhibitor (BPTI) has been crystallised, and the X-ray structure has been solved using the molecular replacement method. The crystals are hexagonal and belong to space group P6(1)22 with lattice parameters of a = b = 83.12 A and c = 222.15 A. Data have been collected to 2.1 A and the structure has been refined to a crystallographic R-factor of 20.6%. Catalysis by salmon trypsin is distinguished by a Km value 20-fold lower than that for mammalian trypsins, and a k(cat) twice as high. The present ST-BPTI complex serves as a model for the Michaelis-Menten complex, and has been compared with corresponding bovine and rat trypsin (RT) complexes. The binding of BPTI to salmon trypsin is characterised by stronger primary interactions in the active site, and a somewhat looser secondary binding.

PubMed: 9760170
DOI: 10.1046/j.1432-1327.1998.2560317.x

実験手法

X-RAY DIFFRACTION (2.1 Å)