2b9l

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

2b9l is a 1 chain structure with sequence from Holotrichia diomphalia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kwon TH, Kim MS, Choi HW, Joo CH, Cho MY, Lee BL. A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem. 2000 Oct;267(20):6188-96. PMID:11012672 doi:10.1046/j.1432-1327.2000.01695.x
↑ Kim MS, Baek MJ, Lee MH, Park JW, Lee SY, Soderhall K, Lee BL. A new easter-type serine protease cleaves a masquerade-like protein during prophenoloxidase activation in Holotrichia diomphalia larvae. J Biol Chem. 2002 Oct 18;277(42):39999-40004. PMID:12185078 doi:10.1074/jbc.M205508200
↑ Piao S, Song YL, Kim JH, Park SY, Park JW, Lee BL, Oh BH, Ha NC. Crystal structure of a clip-domain serine protease and functional roles of the clip domains. EMBO J. 2005 Dec 21;24(24):4404-14. Epub 2005 Dec 15. PMID:16362048
↑ Lee SY, Kwon TH, Hyun JH, Choi JS, Kawabata SI, Iwanaga S, Lee BL. In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. Eur J Biochem. 1998 May 15;254(1):50-7. PMID:9652393 doi:10.1046/j.1432-1327.1998.2540050.x
↑ Kim MS, Baek MJ, Lee MH, Park JW, Lee SY, Soderhall K, Lee BL. A new easter-type serine protease cleaves a masquerade-like protein during prophenoloxidase activation in Holotrichia diomphalia larvae. J Biol Chem. 2002 Oct 18;277(42):39999-40004. PMID:12185078 doi:10.1074/jbc.M205508200
↑ Piao S, Song YL, Kim JH, Park SY, Park JW, Lee BL, Oh BH, Ha NC. Crystal structure of a clip-domain serine protease and functional roles of the clip domains. EMBO J. 2005 Dec 21;24(24):4404-14. Epub 2005 Dec 15. PMID:16362048

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b9l"

@@ Line 3: / Line 3: @@
 <StructureSection load='2b9l' size='340' side='right'caption='[[2b9l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2b9l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Holdi Holdi]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B9L FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b9l OCA], [http://pdbe.org/2b9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b9l RCSB], [http://www.ebi.ac.uk/pdbsum/2b9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b9l ProSAT]</span></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=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>
+<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>
 </table>
+== Function ==
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/2b9l_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Holdi]]
+[[Category: Holotrichia diomphalia]]
 [[Category: Large Structures]]
-[[Category: Ha, N C]]
+[[Category: Ha N-C]]
-[[Category: Lee, B L]]
+[[Category: Lee BL]]
-[[Category: Oh, B H]]
+[[Category: Oh B-H]]
-[[Category: Park, S Y]]
+[[Category: Park SY]]
-[[Category: Piao, S]]
+[[Category: Piao S]]
-[[Category: Song, Y L]]
+[[Category: Song Y-L]]
-[[Category: Clip domain]]
-[[Category: Easter]]
-[[Category: Immune system-protein binding complex]]
-[[Category: Innate immunity]]
-[[Category: Melanin]]

2b9l

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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