2olg
From Proteopedia
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|PDB= 2olg |SIZE=350|CAPTION= <scene name='initialview01'>2olg</scene>, resolution 1.70Å | |PDB= 2olg |SIZE=350|CAPTION= <scene name='initialview01'>2olg</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2b9l|2B9L]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2olg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olg OCA], [http://www.ebi.ac.uk/pdbsum/2olg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2olg RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Ha, N C.]] | [[Category: Ha, N C.]] | ||
[[Category: Piao, S.]] | [[Category: Piao, S.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: SO4]] | ||
[[Category: ppaf-i]] | [[Category: ppaf-i]] | ||
[[Category: prophenoloxidase activating factor-i]] | [[Category: prophenoloxidase activating factor-i]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:31 2008'' |
Revision as of 01:19, 31 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 2B9L
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form
Overview
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
2OLG is a Single protein structure of sequence from Holotrichia diomphalia. Full crystallographic information is available from OCA.
Reference
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:17287215
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