3OFW
Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Carribean sea anemone stichodactyla helianthus
Summary for 3OFW
| Entry DOI | 10.2210/pdb3ofw/pdb |
| Related | 3M7Q |
| Descriptor | Kunitz-type proteinase inhibitor SHPI-1, CHLORIDE ION (3 entities in total) |
| Functional Keywords | kunitz type, serine protease inhibitor, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Stichodactyla helianthus (Carribean sea anemone) |
| Cellular location | Secreted: P31713 |
| Total number of polymer chains | 1 |
| Total formula weight | 6730.86 |
| Authors | Garcia-Fernandez, R.,Redecke, L.,Pons, T.,Perbandt, M.,Talavera, A.,Gil, D.,Gonzalez, Y.,de los Angeles Chavez, M.,Betzel, C. (deposition date: 2010-08-16, release date: 2011-08-17, Last modification date: 2024-11-20) |
| Primary citation | Garcia-Fernandez, R.,Pons, T.,Meyer, A.,Perbandt, M.,Gonzalez-Gonzalez, Y.,Gil, D.,de los Angeles Chavez, M.,Betzel, C.,Redecke, L. Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus. Acta Crystallogr.,Sect.F, 68:1289-1293, 2012 Cited by PubMed Abstract: The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5 Å resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual ϕ angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of ϕ and ψ angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study. PubMed: 23143234DOI: 10.1107/S1744309112039085 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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