2olg: Difference between revisions
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[[Image:2olg.gif|left|200px]] | [[Image:2olg.gif|left|200px]] | ||
'''Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form''' | {{Structure | ||
|PDB= 2olg |SIZE=350|CAPTION= <scene name='initialview01'>2olg</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OLG is a [ | 2OLG is a [[Single protein]] structure of sequence from [http://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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17287215 17287215] | ||
[[Category: Holotrichia diomphalia]] | [[Category: Holotrichia diomphalia]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:01:16 2008'' | ||
Revision as of 16:01, 20 March 2008
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| 2olg, resolution 1.70Å | |||||||||||||
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| Ligands: | NAG, SO4 and CA | ||||||||||||
| 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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