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2fmj
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2fmj.gif|left|200px]] | + | [[Image:2fmj.gif|left|200px]] |
| - | '''220-loop mutant of streptomyces griseus trypsin''' | + | |
| + | {{Structure | ||
| + | |PDB= 2fmj |SIZE=350|CAPTION= <scene name='initialview01'>2fmj</scene>, resolution 1.65Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | ||
| + | |GENE= sprT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 Streptomyces griseus]) | ||
| + | }} | ||
| + | |||
| + | '''220-loop mutant of streptomyces griseus trypsin''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 6: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2FMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus | + | 2FMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMJ OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 30: | ||
[[Category: trypsin]] | [[Category: trypsin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:14 2008'' |
Revision as of 14:54, 20 March 2008
| |||||||
| , 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
Categories: Single protein | Streptomyces griseus | Trypsin | Cera, E Di. | Page, M J. | CA | SO4 | Serine protease
