2fmj

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[[Image:2fmj.gif|left|200px]]
[[Image:2fmj.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2fmj |SIZE=350|CAPTION= <scene name='initialview01'>2fmj</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_2fmj", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= sprT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 Streptomyces griseus])
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-->
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|DOMAIN=
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{{STRUCTURE_2fmj| PDB=2fmj | SCENE= }}
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|RELATEDENTRY=[[1sgt|1SGT]], [[1os8|1OS8]], [[1oss|1OSS]]
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|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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}}
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'''220-loop mutant of streptomyces griseus trypsin'''
'''220-loop mutant of streptomyces griseus trypsin'''
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[[Category: Cera, E Di.]]
[[Category: Cera, E Di.]]
[[Category: Page, M J.]]
[[Category: Page, M J.]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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[[Category: trypsin]]
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[[Category: Trypsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:04:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:04:51 2008''
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Revision as of 01:04, 4 May 2008

Image:2fmj.gif

Template:STRUCTURE 2fmj

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 Sun May 4 04:04:20 2008

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