2b9l

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(New page: 200px<br /><applet load="2b9l" size="350" color="white" frame="true" align="right" spinBox="true" caption="2b9l, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:2b9l.gif|left|200px]]<br /><applet load="2b9l" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2b9l, resolution 2.00&Aring;" />
 
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'''Crystal structure of prophenoloxidase activating factor-II from the beetle Holotrichia diomphalia'''<br />
 
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==Overview==
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==Crystal structure of prophenoloxidase activating factor-II from the beetle Holotrichia diomphalia==
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Clip-domain serine proteases (SPs) are the essential components of, extracellular signaling cascades in various biological processes, especially in embryonic development and the innate immune responses of, invertebrates. They consist of a chymotrypsin-like SP domain and one or, two clip domains at the N-terminus. Prophenoloxidase-activating factor, (PPAF)-II, which belongs to the noncatalytic clip-domain SP family, is, indispensable for the generation of the active phenoloxidase leading to, melanization, a major defense mechanism of insects. Here, the crystal, structure of PPAF-II reveals that the clip domain adopts a novel fold, containing a central cleft, which is distinct from the structures of, defensins with a similar arrangement of cysteine residues. Ensuing studies, demonstrated that PPAF-II forms a homo-oligomer upon cleavage by the, upstream protease and that the clip domain of PPAF-II functions as a, module for binding phenoloxidase through the central cleft, while the clip, domain of a catalytically active easter-type SP plays an essential role in, the rapid activation of its protease domain.
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<StructureSection load='2b9l' size='340' side='right'caption='[[2b9l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2b9l]] 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=2B9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B9L FirstGlance]. <br>
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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]] 2&#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=FUC:ALPHA-L-FUCOSE'>FUC</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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b9l OCA], [https://pdbe.org/2b9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b9l RCSB], [https://www.ebi.ac.uk/pdbsum/2b9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b9l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPAF2_HOLDI PPAF2_HOLDI] Binds and activates processed prophenoloxidases PPO1 and PPO2 and thus is involved in the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products.<ref>PMID:11012672</ref> <ref>PMID:12185078</ref> <ref>PMID:16362048</ref> <ref>PMID:9652393</ref> <ref>PMID:12185078</ref>
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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/b9/2b9l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2b9l 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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Clip-domain serine proteases (SPs) are the essential components of extracellular signaling cascades in various biological processes, especially in embryonic development and the innate immune responses of invertebrates. They consist of a chymotrypsin-like SP domain and one or two clip domains at the N-terminus. Prophenoloxidase-activating factor (PPAF)-II, which belongs to the noncatalytic clip-domain SP family, is indispensable for the generation of the active phenoloxidase leading to melanization, a major defense mechanism of insects. Here, the crystal structure of PPAF-II reveals that the clip domain adopts a novel fold containing a central cleft, which is distinct from the structures of defensins with a similar arrangement of cysteine residues. Ensuing studies demonstrated that PPAF-II forms a homo-oligomer upon cleavage by the upstream protease and that the clip domain of PPAF-II functions as a module for binding phenoloxidase through the central cleft, while the clip domain of a catalytically active easter-type SP plays an essential role in the rapid activation of its protease domain.
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==About this Structure==
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Crystal structure of a clip-domain serine protease and functional roles of the clip domains.,Piao S, Song YL, Kim JH, Park SY, Park JW, Lee BL, Oh BH, Ha NC EMBO J. 2005 Dec 21;24(24):4404-14. Epub 2005 Dec 15. PMID:16362048<ref>PMID:16362048</ref>
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2B9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Holotrichia_diomphalia Holotrichia diomphalia] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B9L 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 a clip-domain serine protease and functional roles of the clip domains., Piao S, Song YL, Kim JH, Park SY, Park JW, Lee BL, Oh BH, Ha NC, EMBO J. 2005 Dec 21;24(24):4404-14. Epub 2005 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16362048 16362048]
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</div>
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<div class="pdbe-citations 2b9l" 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 N-C]]
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[[Category: Lee, B.L.]]
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[[Category: Lee BL]]
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[[Category: Oh, B.H.]]
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[[Category: Oh B-H]]
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[[Category: Park, S.Y.]]
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[[Category: Park SY]]
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[[Category: Piao, S.]]
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[[Category: Piao S]]
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[[Category: Song, Y.L.]]
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[[Category: Song Y-L]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: clip domain]]
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[[Category: easter]]
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[[Category: innate immunity]]
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[[Category: melanin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:19:36 2008''
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Current revision

Crystal structure of prophenoloxidase activating factor-II from the beetle Holotrichia diomphalia

PDB ID 2b9l

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