1bzx

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1bzx, resolution 2.1Å

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

Overview

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.

About this Structure

1BZX is a Protein complex structure of sequences from Bos taurus and Salmo salar with CA as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor., Helland R, Leiros I, Berglund GI, Willassen NP, Smalas AO, Eur J Biochem. 1998 Sep 1;256(2):317-24. PMID:9760170

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