EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.1.4 | group-IB sPLA2 expressed from Escherichia coli | Sus scrofa |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.1.4 | group-IB secreted sPLA2 complexed with 12 molecules of octyl sulfate (C8S), by hanging drop vapor diffusion method at 25°C, to 2.7 A resolution. Crystal form-1 belongs to space group P212121 with unit cell paramteters a = 66.0 A, b = 82.1 A, c = 123.8 A, with four protein subunits in the asymmetric unit. Crystal form-2 belongs to space group P3121 with unit cell paramteters a = 66.1 A, b = 69.1 A, c = 68.8 A, with one subunit in the asymmetric unit. Main difference of crystallization conditions between the two crystal forms is the presence of 20% (v/v) isopropanol in crystal form-2. Alkyl tails of the C8S molecules are centered in the middle of the tetrameric cluster of sPLA2 subunits. Three of the four sPLA2 subunits contain a C8S molecule in the active site pocket. Sulfate oxygen of a C8S ligand is complexed to the active site calcium in three of the four protein active sites. Interactions of the alkyl sulfate head group with Arg-6 and Lys-10, as well as the backbone amide of Met-20. Cluster of three anions in the structure is postulated to be the site for nucleating the binding of anionic amphiphiles to the interfacial surface of the protein, and therefore this binding interaction has implications for interfacial activation of the enzyme | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.4 | Sus scrofa | P00592 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.1.4 | pancreas | - |
Sus scrofa | - |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.1.4 | homotetramer | crystal form-1, crystallography | Sus scrofa |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.4 | phospholipase A2 | - |
Sus scrofa |
3.1.1.4 | sPLA2 | - |
Sus scrofa |