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[[Image:2fmj.gif|left|200px]]


{{Structure
==220-loop mutant of streptomyces griseus trypsin==
|PDB= 2fmj |SIZE=350|CAPTION= <scene name='initialview01'>2fmj</scene>, resolution 1.65&Aring;
<StructureSection load='2fmj' size='340' side='right'caption='[[2fmj]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[2fmj]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FMJ FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
|GENE= sprT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 Streptomyces griseus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmj OCA], [https://pdbe.org/2fmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fmj RCSB], [https://www.ebi.ac.uk/pdbsum/2fmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRYP_STRGR TRYP_STRGR]  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/2fmj_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fmj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''220-loop mutant of streptomyces griseus trypsin'''
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<ref>PMID:16503653</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fmj" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Trypsin 3D structures|Trypsin 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16503653 16503653]
[[Category: Single protein]]
[[Category: Streptomyces griseus]]
[[Category: Streptomyces griseus]]
[[Category: Trypsin]]
[[Category: Di Cera E]]
[[Category: Cera, E Di.]]
[[Category: Page MJ]]
[[Category: Page, M J.]]
[[Category: CA]]
[[Category: SO4]]
[[Category: serine protease]]
[[Category: trypsin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:14 2008''
Retrieved from "https://proteopedia.org/2fmj"