2FMJ
220-loop mutant of streptomyces griseus trypsin
Summary for 2FMJ
| Entry DOI | 10.2210/pdb2fmj/pdb |
| Related | 1OS8 1OSS 1SGT |
| Descriptor | Trypsin, CALCIUM ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | trypsin, serine protease, hydrolase |
| Biological source | Streptomyces griseus |
| Total number of polymer chains | 1 |
| Total formula weight | 23191.88 |
| Authors | Page, M.J.,Di Cera, E. (deposition date: 2006-01-09, release date: 2006-05-23, Last modification date: 2024-10-30) |
| Primary citation | Page, M.J.,Bleackley, M.R.,Wong, S.,MacGillivray, R.T.,Di Cera, E. Conversion of trypsin into a Na(+)-activated enzyme. Biochemistry, 45:2987-2993, 2006 Cited by PubMed Abstract: 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. PubMed: 16503653DOI: 10.1021/bi052481a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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