2olg
From Proteopedia
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| , resolution 1.70Å | |||||||
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| Ligands: | , and | ||||||
| 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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