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2fmj
From Proteopedia
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|PDB= 2fmj |SIZE=350|CAPTION= <scene name='initialview01'>2fmj</scene>, resolution 1.65Å | |PDB= 2fmj |SIZE=350|CAPTION= <scene name='initialview01'>2fmj</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= sprT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 Streptomyces griseus]) | |GENE= sprT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 Streptomyces griseus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sgt|1SGT]], [[1os8|1OS8]], [[1oss|1OSS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmj OCA], [http://www.ebi.ac.uk/pdbsum/2fmj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fmj RCSB]</span> | ||
}} | }} | ||
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[[Category: Cera, E Di.]] | [[Category: Cera, E Di.]] | ||
[[Category: Page, M J.]] | [[Category: Page, M J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: SO4]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
[[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 Mon Mar 31 03:04:51 2008'' |
Revision as of 00:04, 31 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | sprT (Streptomyces griseus) | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Related: | 1SGT, 1OS8, 1OSS
| ||||||
| 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
