Please use this identifier to cite or link to this item: https://doi.org/10.1107/S1744309109014420
Title: Crystallization of a nonclassical Kazal-type Carcinoscorpius rotundicauda serine protease inhibitor, CrSPI-1, complexed with subtilisin
Authors: Tulsidas, S.R.
Thangamani, S. 
Ho, B.
Sivaraman, J. 
Ding, J.L. 
Keywords: CrSPI
Horseshoe crab
Host-pathogen interaction
Immune defence
Kazal-type serine protease inhibitors
Serine proteases
Issue Date: 2009
Citation: Tulsidas, S.R., Thangamani, S., Ho, B., Sivaraman, J., Ding, J.L. (2009). Crystallization of a nonclassical Kazal-type Carcinoscorpius rotundicauda serine protease inhibitor, CrSPI-1, complexed with subtilisin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 65 (5) : 533-535. ScholarBank@NUS Repository. https://doi.org/10.1107/S1744309109014420
Abstract: Serine proteases play a major role in host-pathogen interactions. The innate immune system is known to respond to invading pathogens in a nonspecific manner. The serine protease cascade is an essential component of the innate immune system of the horseshoe crab. The serine protease inhibitor CrSPI isoform 1 (CrSPI-1), a unique nonclassical Kazal-type inhibitor of molecular weight 9.3 kDa, was identified from the hepatopancreas of the horseshoe crab Carcinoscorpius rotundicauda. It potently inhibits subtilisin and constitutes a powerful innate immune defence against invading microbes. Here, the cloning, expression, purification and cocrystallization of CrSPI-1 with subtilisin are reported. The crystals diffracted to 2.6 Å resolution and belonged to space group P21, with unit-cell parameters a = 73.8, b = 65.0, c = 111.9 Å, Β = 95.4°. The Matthews coefficient (V M = 2.64 Å3 Da-1, corresponding to 53% solvent content) and analysis of the preliminary structure solution indicated the presence of one heterotrimer (1:2 ratio of CrSPI-1:subtilisin) and one free subtilisin molecule in the asymmetric unit. © 2009 International Union of Crystallography. All right reserved.
Source Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/100377
ISSN: 17443091
DOI: 10.1107/S1744309109014420
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