2fmj

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spinqualitylabelsall models PDB ID 2fmj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.65Å
Ligands:	and
Gene:	sprT (Streptomyces griseus)
Activity:	Trypsin, with EC number 3.4.21.4
Coordinates:	save as pdb, mmCIF, xml

220-loop mutant of streptomyces griseus trypsin

Overview

Serine proteases of the chymotrypsin family show a dichotomous amino acid distribution for residue 225. Enzymes carrying Tyr at position 225 are activated by Na(+), whereas those carrying Pro are devoid of Na(+) binding and activation. Previous studies have demonstrated that the Y225P conversion is sufficient to abrogate Na(+) activation in several enzymes. However, the reverse substitution P225Y is necessary but not sufficient to introduce Na(+) binding and activation. Here we report that Streptomyces griseus trypsin, carrying Pro-225, can be engineered into a Na(+)-activated enzyme by replacing residues in the 170, 186, and 220 loops to those of coagulation factor Xa. The findings represent the first instance of an engineered Na(+)-activated enzyme and a proof of principle that should enable the design of other proteases with enhanced catalytic activity and allosteric regulation mediated by monovalent cation binding.

About this Structure

2FMJ is a Single protein structure of sequence from Streptomyces griseus. Full crystallographic information is available from OCA.

Reference

Conversion of trypsin into a Na(+)-activated enzyme., Page MJ, Bleackley MR, Wong S, MacGillivray RT, Di Cera E, Biochemistry. 2006 Mar 7;45(9):2987-93. PMID:16503653

Page seeded by OCA on Thu Mar 20 16:54:14 2008