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


{{Structure
==Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form==
|PDB= 2olg |SIZE=350|CAPTION= <scene name='initialview01'>2olg</scene>, resolution 1.70&Aring;
<StructureSection load='2olg' size='340' side='right'caption='[[2olg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[2olg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Holotrichia_diomphalia Holotrichia diomphalia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OLG FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2olg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olg OCA], [https://pdbe.org/2olg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2olg RCSB], [https://www.ebi.ac.uk/pdbsum/2olg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2olg ProSAT]</span></td></tr>
 
</table>
'''Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form'''
== Function ==
 
[https://www.uniprot.org/uniprot/PPAF1_HOLDI PPAF1_HOLDI] Serine endopeptidase which, by cleaving prophenoloxidase PPO1 and PPO2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products.<ref>PMID:12185078</ref> <ref>PMID:16362048</ref> <ref>PMID:17287215</ref> <ref>PMID:9652393</ref> <ref>PMID:9839951</ref>  
 
== Evolutionary Conservation ==
==Overview==
[[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/ol/2olg_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=2olg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A family of serine proteases (SPs) mediates the proteolytic cascades of embryonic development and immune response in invertebrates. These proteases, called easter-type SPs, consist of clip and chymotrypsin-like SP domains. The SP domain of easter-type proteases differs from those of typical SPs in its primary structure. Herein, we report the first crystal structure of the SP domain of easter-type proteases, presented as that of prophenoloxidase activating factor (PPAF)-I in zymogen form. This structure reveals several important structural features including a bound calcium ion, an additional loop with a unique disulfide linkage, a canyon-like deep active site, and an exposed activation loop. We subsequently show the role of the bound calcium and the proteolytic susceptibility of the activation loop, which occurs in a clip domain-independent manner. Based on biochemical study in the presence of heparin, we suggest that PPAF-III, highly homologous to PPAF-I, contains a surface patch that is responsible for enhancing the catalytic activity through interaction with a nonsubstrate region of a target protein. These results provide insights into an activation mechanism of easter-type proteases in proteolytic cascades, in comparison with the well studied blood coagulation enzymes in mammals.
A family of serine proteases (SPs) mediates the proteolytic cascades of embryonic development and immune response in invertebrates. These proteases, called easter-type SPs, consist of clip and chymotrypsin-like SP domains. The SP domain of easter-type proteases differs from those of typical SPs in its primary structure. Herein, we report the first crystal structure of the SP domain of easter-type proteases, presented as that of prophenoloxidase activating factor (PPAF)-I in zymogen form. This structure reveals several important structural features including a bound calcium ion, an additional loop with a unique disulfide linkage, a canyon-like deep active site, and an exposed activation loop. We subsequently show the role of the bound calcium and the proteolytic susceptibility of the activation loop, which occurs in a clip domain-independent manner. Based on biochemical study in the presence of heparin, we suggest that PPAF-III, highly homologous to PPAF-I, contains a surface patch that is responsible for enhancing the catalytic activity through interaction with a nonsubstrate region of a target protein. These results provide insights into an activation mechanism of easter-type proteases in proteolytic cascades, in comparison with the well studied blood coagulation enzymes in mammals.


==About this Structure==
Crystal structure of the serine protease domain of prophenoloxidase activating factor-I.,Piao S, Kim S, Kim JH, Park JW, Lee BL, Ha NC J Biol Chem. 2007 Apr 6;282(14):10783-91. Epub 2007 Feb 7. PMID:17287215<ref>PMID:17287215</ref>
2OLG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Holotrichia_diomphalia Holotrichia diomphalia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of the serine protease domain of prophenoloxidase activating factor-I., Piao S, Kim S, Kim JH, Park JW, Lee BL, Ha NC, J Biol Chem. 2007 Apr;282(14):10783-91. Epub 2007 Feb 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17287215 17287215]
</div>
<div class="pdbe-citations 2olg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Holotrichia diomphalia]]
[[Category: Holotrichia diomphalia]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ha, N C.]]
[[Category: Ha NC]]
[[Category: Piao, S.]]
[[Category: Piao S]]
[[Category: CA]]
[[Category: NAG]]
[[Category: SO4]]
[[Category: ppaf-i]]
[[Category: prophenoloxidase activating factor-i]]
[[Category: serine protease]]
 
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Retrieved from "https://proteopedia.org/2olg"