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2olg

From Proteopedia

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Current revision

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

Structural highlights

2olg 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 1.7Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[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

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.

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^[6]

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

References

↑ 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
↑ Piao S, Kim S, Kim JH, Park JW, Lee BL, Ha NC. Crystal structure of the serine protease domain of prophenoloxidase activating factor-I. J Biol Chem. 2007 Apr 6;282(14):10783-91. Epub 2007 Feb 7. PMID:17287215 doi:10.1074/jbc.M611556200
↑ 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
↑ Lee SY, Cho MY, Hyun JH, Lee KM, Homma KI, Natori S, Kawabata SI, Iwanaga S, Lee BL. Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem. 1998 Nov 1;257(3):615-21. PMID:9839951 doi:10.1046/j.1432-1327.1998.2570615.x
↑ Piao S, Kim S, Kim JH, Park JW, Lee BL, Ha NC. Crystal structure of the serine protease domain of prophenoloxidase activating factor-I. J Biol Chem. 2007 Apr 6;282(14):10783-91. Epub 2007 Feb 7. PMID:17287215 doi:10.1074/jbc.M611556200

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/2olg"

Categories: Holotrichia diomphalia | Large Structures | Ha NC | Piao S

@@ Line 3: / Line 3: @@
 <StructureSection load='2olg' size='340' side='right'caption='[[2olg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2olg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Holdi Holdi]. 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>
+<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>
-</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=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]] 1.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b9l|2b9l]]</div></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=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>
+== 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Holdi]]
+[[Category: Holotrichia diomphalia]]
 [[Category: Large Structures]]
-[[Category: Ha, N C]]
+[[Category: Ha NC]]
-[[Category: Piao, S]]
+[[Category: Piao S]]
-[[Category: Hydrolase]]
-[[Category: Ppaf-i]]
-[[Category: Prophenoloxidase activating factor-i]]
-[[Category: Serine protease]]

2olg

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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