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2olg

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[[Image:2olg.gif|left|200px]]
 
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==Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form==
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The line below this paragraph, containing "STRUCTURE_2olg", creates the "Structure Box" on the page.
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<StructureSection load='2olg' size='340' side='right'caption='[[2olg]], [[Resolution|resolution]] 1.70&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'>[[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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_2olg| PDB=2olg | SCENE= }}
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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=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>
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</table>
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'''Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form'''
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== Function ==
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[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>
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== Evolutionary Conservation ==
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==Overview==
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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/ol/2olg_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=2olg 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 ==
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.
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==About this Structure==
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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>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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<div class="pdbe-citations 2olg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Holotrichia diomphalia]]
[[Category: Holotrichia diomphalia]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ha, N C.]]
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[[Category: Ha NC]]
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[[Category: Piao, S.]]
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[[Category: Piao S]]
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[[Category: Ppaf-i]]
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[[Category: Prophenoloxidase activating factor-i]]
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[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:09:29 2008''
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Current revision

Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form

PDB ID 2olg

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