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2fmj

From Proteopedia

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[[Image:2fmj.gif|left|200px]]
 
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==220-loop mutant of streptomyces griseus trypsin==
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The line below this paragraph, containing "STRUCTURE_2fmj", creates the "Structure Box" on the page.
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<StructureSection load='2fmj' size='340' side='right'caption='[[2fmj]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2fmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914]. 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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><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>
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-->
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sgt|1sgt]], [[1os8|1os8]], [[1oss|1oss]]</div></td></tr>
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{{STRUCTURE_2fmj| PDB=2fmj | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sprT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 "Actinomyces griseus" Krainsky 1914])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>
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<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>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/2fmj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''220-loop mutant of streptomyces griseus trypsin'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2fmj" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Actinomyces griseus krainsky 1914]]
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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]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Streptomyces griseus]]
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[[Category: Trypsin]]
[[Category: Trypsin]]
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[[Category: Cera, E Di.]]
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[[Category: Cera, E Di]]
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[[Category: Page, M J.]]
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[[Category: Page, M J]]
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[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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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''
 

Current revision

220-loop mutant of streptomyces griseus trypsin

PDB ID 2fmj

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