2fmj

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[[Image:2fmj.gif|left|200px]]<br /><applet load="2fmj" size="350" color="white" frame="true" align="right" caption="2fmj, resolution 1.65&Aring;" />
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[[Image:2fmj.gif|left|200px]]
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'''220-loop mutant of streptomyces griseus trypsin'''<br />
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{{Structure
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|PDB= 2fmj |SIZE=350|CAPTION= <scene name='initialview01'>2fmj</scene>, resolution 1.65&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|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]
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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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'''220-loop mutant of streptomyces griseus trypsin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [[ligands]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMJ OCA].
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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==
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[[Category: trypsin]]
[[Category: trypsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 18 20:00:14 2008''
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''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

Image:2fmj.gif


PDB ID 2fmj

Drag the structure with the mouse to rotate
, 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

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