2fmj
From Proteopedia
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| , resolution 1.65Å | |||||||
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| Ligands: | , | ||||||
| Gene: | sprT (Streptomyces griseus) | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Related: | 1SGT, 1OS8, 1OSS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 03:04:51 2008
